| pubmed-article:10899782 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10899782 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:10899782 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
| pubmed-article:10899782 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
| pubmed-article:10899782 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10899782 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:10899782 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:10899782 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10899782 | pubmed:dateCreated | 2000-9-14 | lld:pubmed |
| pubmed-article:10899782 | pubmed:abstractText | The structure of a complex between the hemagglutinin of influenza virus and the Fab of a neutralizing antibody was determined by X-ray crystallography at 2.8 A resolution. This antibody and another which has only 56% sequence identity bind to the same epitope with very similar affinities and in the same orientation. One third of the interactions is conserved in the two complexes; a significant proportion of the interactions that differ are established by residues of the H3 complementarity-determining regions (CDR) which adopt distinct conformations in the two antibodies. This demonstrates that there is a definite flexibility in the selection of antibodies that bind to a given epitope, despite the high affinity of their complexes. This flexibility allows the humoral immune response to be redundant, a feature that may be useful in achieving longer lasting protection against evolving viral pathogens. | lld:pubmed |
| pubmed-article:10899782 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10899782 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10899782 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10899782 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10899782 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10899782 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10899782 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10899782 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10899782 | pubmed:issn | 0887-3585 | lld:pubmed |
| pubmed-article:10899782 | pubmed:author | pubmed-author:SkehelJ JJJ | lld:pubmed |
| pubmed-article:10899782 | pubmed:author | pubmed-author:FleuryDD | lld:pubmed |
| pubmed-article:10899782 | pubmed:author | pubmed-author:DanielsR SRS | lld:pubmed |
| pubmed-article:10899782 | pubmed:author | pubmed-author:KnossowMM | lld:pubmed |
| pubmed-article:10899782 | pubmed:author | pubmed-author:BizebardTT | lld:pubmed |
| pubmed-article:10899782 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10899782 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:10899782 | pubmed:volume | 40 | lld:pubmed |
| pubmed-article:10899782 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10899782 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10899782 | pubmed:pagination | 572-8 | lld:pubmed |
| pubmed-article:10899782 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10899782 | pubmed:meshHeading | pubmed-meshheading:10899782... | lld:pubmed |
| pubmed-article:10899782 | pubmed:meshHeading | pubmed-meshheading:10899782... | lld:pubmed |
| pubmed-article:10899782 | pubmed:meshHeading | pubmed-meshheading:10899782... | lld:pubmed |
| pubmed-article:10899782 | pubmed:meshHeading | pubmed-meshheading:10899782... | lld:pubmed |
| pubmed-article:10899782 | pubmed:meshHeading | pubmed-meshheading:10899782... | lld:pubmed |
| pubmed-article:10899782 | pubmed:meshHeading | pubmed-meshheading:10899782... | lld:pubmed |
| pubmed-article:10899782 | pubmed:meshHeading | pubmed-meshheading:10899782... | lld:pubmed |
| pubmed-article:10899782 | pubmed:meshHeading | pubmed-meshheading:10899782... | lld:pubmed |
| pubmed-article:10899782 | pubmed:meshHeading | pubmed-meshheading:10899782... | lld:pubmed |
| pubmed-article:10899782 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10899782 | pubmed:articleTitle | Structural evidence for recognition of a single epitope by two distinct antibodies. | lld:pubmed |
| pubmed-article:10899782 | pubmed:affiliation | Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, France. | lld:pubmed |
| pubmed-article:10899782 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10899782 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:385120 | entrezgene:pubmed | pubmed-article:10899782 | lld:entrezgene |
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