rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
6139
|
pubmed:dateCreated |
1987-11-9
|
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.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0028-0836
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
329
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
506-12
|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3309677-Antigens,
pubmed-meshheading:3309677-Binding Sites,
pubmed-meshheading:3309677-Computer Graphics,
pubmed-meshheading:3309677-Glycoproteins,
pubmed-meshheading:3309677-HLA Antigens,
pubmed-meshheading:3309677-HLA-A2 Antigen,
pubmed-meshheading:3309677-Humans,
pubmed-meshheading:3309677-Membrane Proteins,
pubmed-meshheading:3309677-Models, Molecular,
pubmed-meshheading:3309677-Protein Binding,
pubmed-meshheading:3309677-Protein Conformation,
pubmed-meshheading:3309677-beta 2-Microglobulin
|
pubmed:articleTitle |
Structure of the human class I histocompatibility antigen, HLA-A2.
|
pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|