@article{pmid3182835,

title = {Preliminary crystallographic data, primary sequence, and binding data for an anti-peptide Fab and its complex with a synthetic peptide from influenza virus hemagglutinin},

author = {U Schulze-Gahmen and J M Rini and J Arevalo and E A Stura and J H Kenten and I A Wilson},

issn = {0021-9258},

year  = {1988},

date = {1988-11-01},

journal = {J Biol Chem},

volume = {263},

number = {32},

pages = {17100--17105},

abstract = {X-ray quality crystals which diffract to high resolution (less than or equal to 1.9-2.1 A) have been grown of an anti-peptide Fab and its complex with a 9-residue peptide antigen. Both crystals are monoclinic P2(1), with unit cell dimensions a = 90.3 A, b = 82.9 A, c = 73.4 A, beta = 122.5 degrees for the native Fab and a = 63.9 A, b = 73.0 A, c = 49.1 A, beta = 120.6 degrees for the complex. The peptide sequence corresponds to residues 100-108 of all influenza virus hemagglutinins (HA1) of the H3 subtype (1968-1987). The peptide antigen has been well characterized immunologically (Wilson, I.A., Niman, H.L., Houghton, R.A., Cherenson, A.R., Connolly, M.L., and Lerner, R.A. (1984) Cell 37, 767-778; Wilson, I.A., Bergmann, K.F., and Stura, E.A. (1986) in Vaccines '86 (Channock, R.M., Lerner, R.A., and Brown, F., eds) pp. 33-37, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY), structurally, as a free peptide by NMR (Dyson, J.H., Cross, K.J., Houghton, R.A., Wilson, I.A., Wright, P.E., and Lerner, R.A. (1985) Nature 318, 480-483; Dyson, J.H., Lerner, R.A., and Wright, P.E., (1988) Annu. Rev. Biophys. Chem. 17, 305-324), as part of the intact antigen by x-ray crystallography (Wilson, I.A., Skehel, J.J., and Wiley, D. C. (1981) Nature 289, 366-373) and by binding studies to the HA molecule (White, J.M., and Wilson, I.A. (1987) J. Cell Biol. 105, 2887-2896). Knowledge of the three-dimensional structure of the complex will elucidate the details of how anti-peptide antibodies recognize a small peptide antigen and provide insights into the recognition of the same sequence in the intact protein antigen. As both native Fab and the peptide-Fab complex have been crystallized, we can also determine in addition whether changes in the structure of the antibody accompany antigen binding. The nucleotide sequence of the mRNA coding region of the anti-peptide Fab has been determined to provide the amino acid sequence ultimately required for the high resolution three-dimensional structure determination.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid2455217,

title = {Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method},

author = {J Field and J Nikawa and D Broek and B MacDonald and L Rodgers and I A Wilson and R A Lerner and M Wigler},

doi = {10.1128/mcb.8.5.2159-2165.1988},

issn = {0270-7306},

year  = {1988},

date = {1988-05-01},

journal = {Mol Cell Biol},

volume = {8},

number = {5},

pages = {2159--2165},

abstract = {We developed a method for immunoaffinity purification of Saccharomyces cerevisiae adenylyl cyclase based on creating a fusion with a small peptide epitope. Using oligonucleotide technology to encode the peptide epitope we constructed a plasmid that expressed the fusion protein from the S. cerevisiae alcohol dehydrogenase promoter ADH1. A monoclonal antibody previously raised against the peptide was used to purify adenylyl cyclase by affinity chromatography. The purified enzyme appeared to be a multisubunit complex consisting of the 200-kilodalton adenylyl cyclase fusion protein and an unidentified 70-kilodalton protein. The purified protein could be activated by RAS proteins. Activation had an absolute requirement for a guanine nucleoside triphosphate.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid3123368,

title = {Analysis of an anti-progesterone antibody: variable crystal morphology of the Fab' and steroid-Fab' complexes},

author = {E A Stura and J H Arevalo and A Feinstein and R B Heap and M J Taussig and I A Wilson},

issn = {0019-2805},

year  = {1987},

date = {1987-12-01},

journal = {Immunology},

volume = {62},

number = {4},

pages = {511--521},

abstract = {Anti-progesterone monoclonal antibodies are being used for structural studies of antibody-antigen interaction, for their ability to block pregnancy shortly after fertilization, and for hormone immunoassay. A mouse anti-progesterone monoclonal Fab' fragment has been crystallized in its native form and co-crystallized with seven different, but structurally related, steroids. The crystals show interesting preferences in their crystal morphology, depending on the bound steroid ligand. The X-ray crystallographic analysis of this Fab', complexed with a series of related steroid ligands, should reveal details of the chemistry of antibody-antigen union and provide insights into how steroids interact with proteins.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid2447101,

title = {Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin},

author = {J M White and I A Wilson},

doi = {10.1083/jcb.105.6.2887},

issn = {0021-9525},

year  = {1987},

date = {1987-12-01},

journal = {J Cell Biol},

volume = {105},

number = {6 Pt 2},

pages = {2887--2896},

abstract = {At low pH, the hemagglutinin (HA) of influenza virus undergoes an irreversible conformational change that potentiates its essential membrane fusion function. We have probed the details of this conformational change using a panel of 14 anti-HA-peptide antibodies. Whereas some antibodies reacted equally well with both the neutral and low-pH HA conformations, others reacted to a significantly greater extent with the low-pH form. The locations of the peptides recognized by the latter antibodies in the three-dimensional HA structure indicated regions of the protein that change in response to low pH. Moreover, kinetic experiments suggested steps in the conformational change. In addition to their relevance to membrane fusion, our results show that anti-peptide antibodies can be used to study some types of biologically important protein conformational changes.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid3315651,

title = {The influenza hemagglutinin precursor as an acid-sensitive probe of the biosynthetic pathway},

author = {F Boulay and R W Doms and I Wilson and A Helenius},

doi = {10.1002/j.1460-2075.1987.tb02555.x},

issn = {0261-4189},

year  = {1987},

date = {1987-09-01},

journal = {EMBO J},

volume = {6},

number = {9},

pages = {2643--2650},

abstract = {The hemagglutinin of influenza virus (HA), an acid-activated membrane fusion protein, is synthesized in the endoplasmic reticulum and transported through the Golgi complex to the cell surface of infected cells as an uncleaved, fusion-incompetent precursor, HA0. The mature, proteolytically activated HA is known to undergo a rapid, irreversible, acid-induced conformational change which mediates membrane fusion and virus penetration. On the basis of antigenic modifications and the acquisition of trypsin susceptibility, we demonstrate here that HA0, while unable to cause fusion, is acid sensitive. It undergoes irreversible conformational changes quite similar to those of HA at mildly acidic pH (pH less than 6.0). The ectodomain of HA0 does not, however, acquire hydrophobic properties and the changes occur in a less concerted manner (the pH dependence is much broader and the rate of conversion slower). These differences are likely to account for the inability of acid-treated HA0 to trigger membrane fusion. It was shown, moreover, that HA0 acquired its acid-sensitive properties immediately following trimerization in the endoplasmic reticulum. Since HA0 did not convert to the acid form at any point during its intracellular transport, we concluded that the trans-Golgi compartment, known to be more acidic than the cytosol and involved in constitutive membrane transport, is not likely to have a pH less than 6.0.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid3593255,

title = {Crystallographic analysis of the three-dimensional structure of baboon alpha-lactalbumin at low resolution. Homology with lysozyme},

author = {S G Smith and M Lewis and R Aschaffenburg and R E Fenna and I A Wilson and M Sundaralingam and D I Stuart and D C Phillips},

doi = {10.1042/bj2420353},

issn = {0264-6021},

year  = {1987},

date = {1987-03-01},

journal = {Biochem J},

volume = {242},

number = {2},

pages = {353--360},

abstract = {The crystal structure of baboon alpha-lactalbumin has been determined at 6 A and at 4.5 A (0.6 nm and 0.45 nm) resolution by the method of isomorphous replacement. The principal derivative was prepared by reducing a disulphide bridge in the crystals and inserting a mercury atom. Detailed comparison of the electron-density maps with corresponding maps of hen egg-white lysozyme shows that they are closely similar, with correlation coefficients of 0.57 and 0.44 at 6 A and 4.5 A resolution respectively. This result, in accordance with earlier predictions based upon comparisons of amino-acid sequences, provides further evidence that class C lysozymes and alpha-lactalbumins are homologous proteins and it is in keeping with the hypothesis that the alpha-lactalbumins evolved from a lysozyme precursor.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid3586022,

title = {Crystallization and preliminary crystallographic data for an antiprogesterone monoclonal antibody Fab' and steroid-Fab' complexes},

author = {E A Stura and A Feinstein and I A Wilson},

doi = {10.1016/0022-2836(87)90642-5},

issn = {0022-2836},

year  = {1987},

date = {1987-01-01},

journal = {J Mol Biol},

volume = {193},

number = {1},

pages = {229--231},

abstract = {Crystals of an Fab' from an antiprogesterone monoclonal antibody (IgG1) have been grown from 1.5 M-ammonium sulfate, pH 5.5 to 8.5. The single crystals are hexagonal rods, space group P6222 (or P6422), with cell dimensions a = b = 135.2 A, and c = 124.2 A. Cocrystals of the Fab' with progesterone, pregnanedione and other related steroids have been grown. The complex crystals have different morphology but are isomorphous with the native crystals. A hydroxy-progesterone derivative obtained by substituting an iodo-benzoyl group at the 11 alpha-hydroxyl position looks promising as a suitable heavy-atom candidate in addition to other potential conventional heavy-atom derivatives. All crystals diffract to at least 2.8 A resolution and are suitable for high-resolution X-ray diffraction studies.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid3525041,

title = {Selection by site-directed antibodies of small regions of peptides which are ordered in water},

author = {H J Dyson and K J Cross and J Ostresh and R A Houghten and I A Wilson and P E Wright and R A Lerner},

doi = {10.1002/9780470513286.ch4},

issn = {0300-5208},

year  = {1986},

date = {1986-01-01},

journal = {Ciba Found Symp},

volume = {119},

pages = {58--75},

abstract = {High resolution nuclear magnetic resonance has been used to study a short peptide which corresponds to the antigenic region of a larger peptide immunogen. This work shows that there is a strong conformational preference for a Type II beta-turn in solution. This observation has implications for the nature of the immunogenicity and antigenicity of peptide antigens as well as for the more general question of protein-folding mechanisms.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid4069219,

title = {The immunodominant site of a synthetic immunogen has a conformational preference in water for a type-II reverse turn},

author = {H J Dyson and K J Cross and R A Houghten and I A Wilson and P E Wright and R A Lerner},

doi = {10.1038/318480a0},

issn = {0028-0836},

year  = {1985},

date = {1985-12-05},

journal = {Nature},

volume = {318},

number = {6045},

pages = {480--483},

abstract = {Many short synthetic peptides have now been shown to induce antibodies reactive with their cognate sequences in the intact folded protein. Aside from the usefulness of such antibodies as site-specific reagents, the frequency with which this recognition occurs has raised several theoretical issues, the central one being that of how an antibody to a short synthetic peptide, which represents one of the most disordered states of a site in a protein, can react with the more ordered version of the same sequence in the folded protein. This apparent paradox can be resolved if the target site on the protein approaches disorder or if the peptide in solution or on a carrier adopts, with significant frequency, a conformation compatible with that of the cognate site in the protein. Various studies already suggest that antigenic sites in proteins correspond to regions of high atomic mobility. We now show, using high-field nuclear magnetic resonance (NMR) spectroscopy, that a nonapeptide selected by several monoclonal antibodies as the immunodominant site of a 36-amino-acid immunogen (residues 75-110 of influenza virus haemagglutinin) adopts a highly populated type-II reverse-turn conformation in water. This suggests that in this case the antibodies have selected a sequence possessing a conformational preference. Apart from helping us to understand immunological recognition, anti-peptide antibodies may provide reagents of sufficient precision for an immunological approach to the problem of protein folding.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid2410917,

title = {Identical short peptide sequences in unrelated proteins can have different conformations: a testing ground for theories of immune recognition},

author = {I A Wilson and D H Haft and E D Getzoff and J A Tainer and R A Lerner and S Brenner},

doi = {10.1073/pnas.82.16.5255},

issn = {0027-8424},

year  = {1985},

date = {1985-08-01},

journal = {Proc Natl Acad Sci U S A},

volume = {82},

number = {16},

pages = {5255--5259},

abstract = {The ability of antibodies raised against disordered short peptides to interact frequently with their cognate sequences in intact folded proteins has raised a major theoretical issue in protein chemistry. We propose to address this issue by using antibodies raised against peptides with identical sequences, but different conformations, in pairs of unrelated proteins of known three-dimensional structure. The general search method presented here enabled us to detect candidate sequences for such immunological studies.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid2581826,

title = {Studies with monoclonal antibodies prepared against X-31 influenza virus haemagglutinin},

author = {J J Skehel and E Brown and R S Daniels and A R Douglas and M Knossow and I A Wilson and N G Wrigley and D C Wiley},

doi = {10.1042/bst0130012},

issn = {0300-5127},

year  = {1985},

date = {1985-02-01},

journal = {Biochem Soc Trans},

volume = {13},

number = {1},

pages = {12--14},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid6204768,

title = {The structure of an antigenic determinant in a protein},

author = {I A Wilson and H L Niman and R A Houghten and A R Cherenson and M L Connolly and R A Lerner},

doi = {10.1016/0092-8674(84)90412-4},

issn = {0092-8674},

year  = {1984},

date = {1984-07-01},

journal = {Cell},

volume = {37},

number = {3},

pages = {767--778},

abstract = {The immunogenic and antigenic determinants of a synthetic peptide and the corresponding antigenic determinants in the parent protein have been elucidated. Four determinants have been defined by reactivity of a large panel of antipeptide monoclonal antibodies with short, overlapping peptides (7-28 amino acids), the immunizing peptide (36 amino acids), and the intact parent protein (the influenza virus hemagglutinin, HA). The majority of the antipeptide antibodies that also react strongly with the intact protein recognize one specific nine amino acid sequence. This immunodominant peptide determinant is located in the subunit interface in the HA trimeric structure. The relative inaccessibility of this site implies that antibody binding to the protein is to a more unfolded HA conformation. This antigenic determinant differs from those previously described for the hemagglutinin and clearly demonstrates the ability of synthetic peptides to generate antibodies that interact with regions of the protein not immunogenic or generally accessible when the protein is the immunogen.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid6584912,

title = {A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody},

author = {J J Skehel and D J Stevens and R S Daniels and A R Douglas and M Knossow and I A Wilson and D C Wiley},

doi = {10.1073/pnas.81.6.1779},

issn = {0027-8424},

year  = {1984},

date = {1984-03-01},

journal = {Proc Natl Acad Sci U S A},

volume = {81},

number = {6},

pages = {1779--1783},

abstract = {A single amino acid substitution, Asp-63 to Asn-63, was detected in the hemagglutinin of an antigenic variant of the 1968 Hong Kong (H3) influenza virus that was selected by growth of the wild-type virus in the presence of a monoclonal antibody. The mutation generates an oligosaccharide attachment site, Asn-Cys-Thr at residues 63-65, that is glycosylated. Immunoprecipitation experiments with extracts from variant virus-infected cells prepared in the presence or absence of tunicamycin, which inhibits glycosylation, demonstrate that addition of the new oligosaccharide side chain is required to prevent reaction with the monoclonal antibody. Similar experiments with the virus of the 1969 Hong Kong influenza epidemic, A/England/878/69, which also contains a hemagglutinin glycosylated at residue 63, support this conclusion and provide evidence for the epidemiological significance of carbohydrate-mediated modifications of hemagglutinin antigenicity.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid6085884,

title = {Structure of antigenic and immunogenic determinants in proteins and synthetic peptides},

author = {I A Wilson},

issn = {0003-472X},

year  = {1984},

date = {1984-01-01},

journal = {Ann Sclavo Collana Monogr},

volume = {1},

number = {2},

pages = {129--138},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid6192445,

title = {Generation of protein-reactive antibodies by short peptides is an event of high frequency: implications for the structural basis of immune recognition},

author = {H L Niman and R A Houghten and L E Walker and R A Reisfeld and I A Wilson and J M Hogle and R A Lerner},

doi = {10.1073/pnas.80.16.4949},

issn = {0027-8424},

year  = {1983},

date = {1983-08-01},

journal = {Proc Natl Acad Sci U S A},

volume = {80},

number = {16},

pages = {4949--4953},

abstract = {Recent studies have shown that chemically synthesized small peptides can induce antibodies that often react with intact proteins regardless of their position in the folded molecule. These findings are difficult to explain in view of the experimental and theoretical data which suggest that in the absence of forces provided by the folded protein, small peptides in aqueous solution do not readily adopt stable structures. In order to rationalize the two findings, there has been general acceptance of a stochastic model which suggests that the multiple conformers of a peptide in solution induce sets of antibodies with a small percentage reactive with conformations shared by the folded protein. This stochastic model has become less tenable as the success rate for the generation of protein-reactive anti-peptide antibodies has grown. To test the stochastic model, we have used monoclonal anti-peptide antibodies as a way of estimating the frequency with which small peptides induce antibodies that react with folded proteins. We have made monoclonal antibodies to six chemically synthesized peptides from three proteins. The frequency with which the peptides induce protein-reactive antibodies is at least 4 orders of magnitude greater than expected from previous experimental work and vastly different from what would be predicted by calculating the possible number of peptide conformers in solution. These findings make the stochastic model less likely and lead to consideration of other models. Aside from their practical significance for generation of highly specific reagents, these findings may have important implications for the protein folding problem.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid6192436,

title = {Sequential mutations in hemagglutinins of influenza B virus isolates: definition of antigenic domains},

author = {M Krystal and J F Young and P Palese and I A Wilson and J J Skehel and D C Wiley},

doi = {10.1073/pnas.80.14.4527},

issn = {0027-8424},

year  = {1983},

date = {1983-07-01},

journal = {Proc Natl Acad Sci U S A},

volume = {80},

number = {14},

pages = {4527--4531},

abstract = {Comparative analysis of the amino acid sequences of hemagglutinins (HAs) of influenza B/Lee/40, B/Md/59, and B/HK/73 viruses has allowed examination of the molecular basis of antigenic variation in type B viruses. As seen with influenza type A viruses, antigenic drift in influenza B viruses proceeds mostly through the accumulation of amino acid substitutions within the HA1 portion of the HA molecule. However, the rate of variation observed among the influenza B virus HAs appears to be significantly lower than the observed rate of variation among influenza A virus HAs. The overall rate of amino acid change in the HA1s of the influenza B viruses studied is 2% per 10 years, whereas the HA1s of H3 influenza A viruses vary by 9.2% per 10 years. The sequences of the influenza B HAs were also examined in relation to the three-dimensional model for the A/Aichi/2/68 HA. When the primary amino acid sequences are compared, it appears that most of the important structural features of the type A HAs--such as the sialic acid binding site, the disulfide linkages, and the stem structure of the trimer--are conserved in the influenza B virus HAs. Regions are also identified where extensive amino acid substitutions have occurred among the three antigenically distinct influenza B virus HAs. The locations of these areas in the B HA structure correspond to antigenic regions proposed for the A virus HAs. In addition, modulation of antigenic regions in B virus HAs may also occur through amino acid deletions and variation in glycosylation sites.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid6873453,

title = {The structure and role of the carbohydrate moieties of influenza virus haemagglutinin},

author = {I A Wilson and R C Ladner and J J Skehel and D C Wiley},

issn = {0300-5127},

year  = {1983},

date = {1983-04-01},

journal = {Biochem Soc Trans},

volume = {11 Pt 2},

pages = {145--147},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid6951181,

title = {Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion},

author = {J J Skehel and P M Bayley and E B Brown and S R Martin and M D Waterfield and J M White and I A Wilson and D C Wiley},

doi = {10.1073/pnas.79.4.968},

issn = {0027-8424},

year  = {1982},

date = {1982-02-01},

journal = {Proc Natl Acad Sci U S A},

volume = {79},

number = {4},

pages = {968--972},

abstract = {A conformational change in the hemagglutinin glycoprotein of influenza virus has been observed to occur to pH values corresponding to those optimal for the membrane fusion activity of the virus. CD, electron microscopic, and sedimentation analyses show that, in the pH range 5.2-4.9, bromelain-solubilized hemagglutinin (BHA) aggregates as protein-protein rosettes and acquires the ability to bind both lipid vesicles and nonionic detergent. Trypsin treatment of BHA in the pH 5.0-induced conformation indicates that aggregation is a property of the BHA2 component and that the conformation change also involves BHA1. The implications of these observations for the role of the glycoprotein in membrane fusion are discussed.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid6115415,

title = {On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase},

author = {T Alber and D W Banner and A C Bloomer and G A Petsko and D Phillips and P S Rivers and I A Wilson},

doi = {10.1098/rstb.1981.0069},

issn = {0962-8436},

year  = {1981},

date = {1981-06-01},

journal = {Philos Trans R Soc Lond B Biol Sci},

volume = {293},

number = {1063},

pages = {159--171},

abstract = {Triose phosphate isomerase is a dimeric enzyme of molecular mass 56 000 which catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate. The crystal structure of the enzyme from chicken muscle has been determined at a resolution of 2.5 A, and an independent determination of the structure of the yeast enzyme has just been completed at 3 A resolution. The conformation of the polypeptide chain is essentially identical in the two structures, and consists of an inner cylinder of eight strands of parallel beta-pleated sheet, with mostly helical segments connecting each strand. The active site is a pocket containing glutamic acid 165, which is believed to act as a base in the reaction. Crystallographic studies of the binding of DHAP to both the chicken and the yeast enzymes reveal a common mode of binding and suggest a mechanisms for catalysis involving polarization of the substrate carbonyl group.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid6162101,

title = {Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation},

author = {D C Wiley and I A Wilson and J J Skehel},

doi = {10.1038/289373a0},

issn = {0028-0836},

year  = {1981},

date = {1981-01-01},

journal = {Nature},

volume = {289},

number = {5796},

pages = {373--378},

abstract = {Four 'antigenic sites' on the three-dimensional structure of the influenza haemagglutinin are identified. At least one amino acid substitution in each site seems to be required for the production of new epidemic strains between 1968 and 1975.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid7464906,

title = {Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution},

author = {I A Wilson and J J Skehel and D C Wiley},

doi = {10.1038/289366a0},

issn = {0028-0836},

year  = {1981},

date = {1981-01-01},

journal = {Nature},

volume = {289},

number = {5796},

pages = {366--373},

abstract = {The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of alpha-helices extends 76 A from the membrane and a globular region of antiparallel beta-sheet, which contains the receptor binding site and the variable antigenic determinants, is positioned on top of this stem. Each subunit has an unusual loop-like topology, starting at the membrane, extending 135 A distally and folding back to enter the membrane.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid650685,

title = {On the protein crystal chemistry of chloroplatinite ions: general principles and interactions with triose phosphate isomerase},

author = {G A Petsko and D C Phillips and R J Williams and I A Wilson},

doi = {10.1016/0022-2836(78)90423-0},

issn = {0022-2836},

year  = {1978},

date = {1978-04-01},

journal = {J Mol Biol},

volume = {120},

number = {3},

pages = {345--359},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid633372,

title = {An analysis of the structure of triose phosphate isomerase and its comparison with lactate dehydrogenase},

author = {D C Phillips and M J Sternberg and J M Thornton and I A Wilson},

doi = {10.1016/0022-2836(78)90440-0},

issn = {0022-2836},

year  = {1978},

date = {1978-02-01},

journal = {J Mol Biol},

volume = {119},

number = {2},

pages = {329--351},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid902882,

title = {An analysis of the three-dimensional structure of chicken triose phosphate isomerase},

author = {D C Phillips and P S Rivers and M J Sternberg and J M Thornton and I A Wilson},

doi = {10.1042/bst0050642},

issn = {0300-5127},

year  = {1977},

date = {1977-01-01},

journal = {Biochem Soc Trans},

volume = {5},

number = {3},

pages = {642--647},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid985462,

title = {Atomic coordinates for triose phosphate isomerase from chicken muscle},

author = {D W Banner and A c Bloomer and G A Petsko and D C Phillips and I A Wilson},

doi = {10.1016/0006-291x(76)90972-4},

issn = {0006-291X},

year  = {1976},

date = {1976-09-01},

journal = {Biochem Biophys Res Commun},

volume = {72},

number = {1},

pages = {146--155},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid3655,

title = {Studies of the histidine residues of triose phosphate isomerase by proton magnetic resonance and x-ray crystallography},

author = {C A Browne and I D Campbell and P A Kiener and D C Phillips and S G Waley and I A Wilson},

doi = {10.1016/s0022-2836(76)80066-6},

issn = {0022-2836},

year  = {1976},

date = {1976-01-01},

journal = {J Mol Biol},

volume = {100},

number = {3},

pages = {319--343},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid1134550,

title = {Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data},

author = {D W Banner and A C Bloomer and G A Petsko and D C Phillips and C I Pogson and I A Wilson and P H Corran and A J Furth and J D Milman and R E Offord and J D Priddle and S G Waley},

doi = {10.1038/255609a0},

issn = {0028-0836},

year  = {1975},

date = {1975-06-01},

journal = {Nature},

volume = {255},

number = {5510},

pages = {609--614},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid6191220,

title = {Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity},

author = {G N Rogers and J C Paulson and R S Daniels and J J Skehel and I A Wilson and D C Wiley},

doi = {10.1038/304076a0},

issn = {0028-0836},

journal = {Nature},

volume = {304},

number = {5921},

pages = {76--78},

abstract = {The haemagglutinin (HA) glycoproteins of influenza virus membranes are responsible for binding viruses to cells by interacting with membrane receptor molecules which contain sialic acid (for review see ref. 1). This interaction is known to vary in detailed specificity for different influenza viruses (see, for example, refs 2-4) and we have attempted to identify the sialic acid binding site of the haemagglutinin by comparing the amino acid sequences of haemagglutinins with different binding specificities. We present here evidence that haemagglutinins which differ in recognizing either NeuAc alpha 2 leads to 3Gal- or NeuAc alpha 2 leads to 6Gal- linkages in glycoproteins also differ at amino acid 226 of HA1. This residue is located in a pocket on the distal tip of the molecule, an area previously proposed from considerations of the three-dimensional structure of the haemagglutinin to be involved in receptor binding.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}