pubmed-article:7538787 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7538787 | lifeskim:mentions | umls-concept:C0032594 | lld:lifeskim |
pubmed-article:7538787 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
pubmed-article:7538787 | lifeskim:mentions | umls-concept:C0021031 | lld:lifeskim |
pubmed-article:7538787 | lifeskim:mentions | umls-concept:C1517880 | lld:lifeskim |
pubmed-article:7538787 | lifeskim:mentions | umls-concept:C0039808 | lld:lifeskim |
pubmed-article:7538787 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
pubmed-article:7538787 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:7538787 | lifeskim:mentions | umls-concept:C0071677 | lld:lifeskim |
pubmed-article:7538787 | lifeskim:mentions | umls-concept:C0349590 | lld:lifeskim |
pubmed-article:7538787 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
pubmed-article:7538787 | lifeskim:mentions | umls-concept:C0231449 | lld:lifeskim |
pubmed-article:7538787 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
pubmed-article:7538787 | pubmed:issue | 20 | lld:pubmed |
pubmed-article:7538787 | pubmed:dateCreated | 1995-6-26 | lld:pubmed |
pubmed-article:7538787 | pubmed:abstractText | The antigen binding fragment from an IgG2a kappa murine monoclonal antibody with specificity for alpha-(2-->8)-linked sialic acid polymers has been prepared and crystallized in the absence of hapten. Crystals were grown by vapor diffusion equilibrium with 16-18% polyethylene glycol 4000 solutions. The structure was solved by molecular replacement methods and refined to a conventional R factor of 0.164 for data to 2.8 A. The binding site is observed to display a shape and distribution of charges that is complementary to that of the predicted conformation of the oligosaccharide epitope. A thermodynamic description of ligand binding has been compiled for oligosaccharides ranging in length from 9 to 41 residues, and the data for the largest ligand has been used in a novel way to estimate the size of the antigen binding site. A model of antigen binding is presented that satisfies this thermodynamic data, as well as a previously reported requirement of conformational specificity of the oligosaccharide. X-ray crystallographic and thermodynamic evidence are consistent with a binding site that accommodates at least eight sialic acid residues. | lld:pubmed |
pubmed-article:7538787 | pubmed:language | eng | lld:pubmed |
pubmed-article:7538787 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7538787 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7538787 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7538787 | pubmed:month | May | lld:pubmed |
pubmed-article:7538787 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:7538787 | pubmed:author | pubmed-author:JenningsH JHJ | lld:pubmed |
pubmed-article:7538787 | pubmed:author | pubmed-author:ORRR TRT | lld:pubmed |
pubmed-article:7538787 | pubmed:author | pubmed-author:FroschMM | lld:pubmed |
pubmed-article:7538787 | pubmed:author | pubmed-author:AltmanEE | lld:pubmed |
pubmed-article:7538787 | pubmed:author | pubmed-author:WeisgerberCC | lld:pubmed |
pubmed-article:7538787 | pubmed:author | pubmed-author:BrissonJ RJR | lld:pubmed |
pubmed-article:7538787 | pubmed:author | pubmed-author:SigurskjoldB... | lld:pubmed |
pubmed-article:7538787 | pubmed:author | pubmed-author:KratzinH DHD | lld:pubmed |
pubmed-article:7538787 | pubmed:author | pubmed-author:EvansS VSV | lld:pubmed |
pubmed-article:7538787 | pubmed:author | pubmed-author:TseW CWC | lld:pubmed |
pubmed-article:7538787 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7538787 | pubmed:day | 23 | lld:pubmed |
pubmed-article:7538787 | pubmed:volume | 34 | lld:pubmed |
pubmed-article:7538787 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7538787 | pubmed:authorsComplete | N | lld:pubmed |
pubmed-article:7538787 | pubmed:pagination | 6737-44 | lld:pubmed |
pubmed-article:7538787 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:7538787 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7538787 | pubmed:articleTitle | Evidence for the extended helical nature of polysaccharide epitopes. The 2.8 A resolution structure and thermodynamics of ligand binding of an antigen binding fragment specific for alpha-(2-->8)-polysialic acid. | lld:pubmed |
pubmed-article:7538787 | pubmed:affiliation | Institute for Biological Sciences, National Research Council of Canada, Ottawa. | lld:pubmed |
pubmed-article:7538787 | pubmed:publicationType | Journal Article | lld:pubmed |
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