| pubmed-article:3309677 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3309677 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:3309677 | lifeskim:mentions | umls-concept:C0019733 | lld:lifeskim |
| pubmed-article:3309677 | lifeskim:mentions | umls-concept:C0019629 | lld:lifeskim |
| pubmed-article:3309677 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:3309677 | pubmed:issue | 6139 | lld:pubmed |
| pubmed-article:3309677 | pubmed:dateCreated | 1987-11-9 | lld:pubmed |
| pubmed-article:3309677 | pubmed:abstractText | The class I histocompatibility antigen from human cell membranes has two structural motifs: the membrane-proximal end of the glycoprotein contains two domains with immunoglobulin-folds that are paired in a novel manner, and the region distal from the membrane is a platform of eight antiparallel beta-strands topped by alpha-helices. A large groove between the alpha-helices provides a binding site for processed foreign antigens. An unknown 'antigen' is found in this site in crystals of purified HLA-A2. | lld:pubmed |
| pubmed-article:3309677 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3309677 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3309677 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3309677 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3309677 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3309677 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3309677 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:3309677 | pubmed:author | pubmed-author:StromingerJ... | lld:pubmed |
| pubmed-article:3309677 | pubmed:author | pubmed-author:SaperM AMA | lld:pubmed |
| pubmed-article:3309677 | pubmed:author | pubmed-author:BjorkmanP JPJ | lld:pubmed |
| pubmed-article:3309677 | pubmed:author | pubmed-author:WileyD CDC | lld:pubmed |
| pubmed-article:3309677 | pubmed:author | pubmed-author:BennettW SWS | lld:pubmed |
| pubmed-article:3309677 | pubmed:author | pubmed-author:SamraouiBB | lld:pubmed |
| pubmed-article:3309677 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3309677 | pubmed:volume | 329 | lld:pubmed |
| pubmed-article:3309677 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3309677 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3309677 | pubmed:pagination | 506-12 | lld:pubmed |
| pubmed-article:3309677 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:3309677 | pubmed:meshHeading | pubmed-meshheading:3309677-... | lld:pubmed |
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| pubmed-article:3309677 | pubmed:meshHeading | pubmed-meshheading:3309677-... | lld:pubmed |
| pubmed-article:3309677 | pubmed:articleTitle | Structure of the human class I histocompatibility antigen, HLA-A2. | lld:pubmed |
| pubmed-article:3309677 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138. | lld:pubmed |
| pubmed-article:3309677 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3309677 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3309677 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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