pubmed-article:8805647 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8805647 | lifeskim:mentions | umls-concept:C1184482 | lld:lifeskim |
pubmed-article:8805647 | lifeskim:mentions | umls-concept:C0003250 | lld:lifeskim |
pubmed-article:8805647 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
pubmed-article:8805647 | lifeskim:mentions | umls-concept:C0019744 | lld:lifeskim |
pubmed-article:8805647 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:8805647 | lifeskim:mentions | umls-concept:C0333051 | lld:lifeskim |
pubmed-article:8805647 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:8805647 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:8805647 | lifeskim:mentions | umls-concept:C2825311 | lld:lifeskim |
pubmed-article:8805647 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:8805647 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
pubmed-article:8805647 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:8805647 | pubmed:dateCreated | 1996-12-12 | lld:pubmed |
pubmed-article:8805647 | pubmed:abstractText | To determine the influence of peptide-binding groove residues and MHC-bound peptide on HLA-B7 conformation, we investigated the binding sites of nine locus- or allele-specific mAbs using a panel of 82 HLA-B7 variants. The functional mAb epitopes encircle the HLA-B7 peptide-binding groove. Three mAbs are affected by mutations at solvent-accessible peptide-binding groove mutations. Mutations in peptide-binding groove residues 45, 63, and 150 affect multiple nonoverlapping mAb epitopes, probably by interaction with other MHC residues or bound peptide. However, 18 of 24 peptide-binding groove mutations do not affect mAb binding, indicating that the conformation of solvent-accessible HLA-B7 structures is largely dissociated from changes in the peptide-binding groove. To test whether bound peptides alter HLA-B7 conformation, we loaded HLA-B7 heavy chains on acid-stripped cells with beta2-microglobulin and 20 individual synthetic peptides. Two of eight mAbs are sensitive to HLA-B7-bound peptides. A likely interpretation of these data is that the conformational flexibility of HLA-B7 is due to peptide-induced conformational shifts in MHC side chains, rather than major shifts in the MHC main chain. These results suggest that HLA-B7 conformation is largely maintained in the context of different bound peptides and different peptide-binding grooves. | lld:pubmed |
pubmed-article:8805647 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8805647 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8805647 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8805647 | pubmed:language | eng | lld:pubmed |
pubmed-article:8805647 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8805647 | pubmed:citationSubset | AIM | lld:pubmed |
pubmed-article:8805647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8805647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8805647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8805647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8805647 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8805647 | pubmed:month | Sep | lld:pubmed |
pubmed-article:8805647 | pubmed:issn | 0022-1767 | lld:pubmed |
pubmed-article:8805647 | pubmed:author | pubmed-author:MogaDD | lld:pubmed |
pubmed-article:8805647 | pubmed:author | pubmed-author:NEVOAA | lld:pubmed |
pubmed-article:8805647 | pubmed:author | pubmed-author:EngelhardV... | lld:pubmed |
pubmed-article:8805647 | pubmed:author | pubmed-author:ValenzuelaAA | lld:pubmed |
pubmed-article:8805647 | pubmed:author | pubmed-author:SmithK DKD | lld:pubmed |
pubmed-article:8805647 | pubmed:author | pubmed-author:BarbosaJ AJA | lld:pubmed |
pubmed-article:8805647 | pubmed:author | pubmed-author:McCutcheonJ... | lld:pubmed |
pubmed-article:8805647 | pubmed:author | pubmed-author:HuczkoEE | lld:pubmed |
pubmed-article:8805647 | pubmed:author | pubmed-author:VignaJ LJL | lld:pubmed |
pubmed-article:8805647 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8805647 | pubmed:day | 15 | lld:pubmed |
pubmed-article:8805647 | pubmed:volume | 157 | lld:pubmed |
pubmed-article:8805647 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8805647 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8805647 | pubmed:pagination | 2470-8 | lld:pubmed |
pubmed-article:8805647 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:8805647 | pubmed:meshHeading | pubmed-meshheading:8805647-... | lld:pubmed |
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pubmed-article:8805647 | pubmed:meshHeading | pubmed-meshheading:8805647-... | lld:pubmed |
pubmed-article:8805647 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8805647 | pubmed:articleTitle | Probing HLA-B7 conformational shifts induced by peptide-binding groove mutations and bound peptide with anti-HLA monoclonal antibodies. | lld:pubmed |
pubmed-article:8805647 | pubmed:affiliation | Department of Pathology, University of Iowa College of Medicine, Iowa City 52242, USA. | lld:pubmed |
pubmed-article:8805647 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8805647 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8805647 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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