Structure of the human class I histocompatibility antigen, HLA-A2
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...
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Published in | Nature (London) Vol. 329; no. 6139; p. 506 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
England
08.10.1987
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Subjects | |
Online Access | Get more information |
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Summary: | 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. |
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ISSN: | 0028-0836 |
DOI: | 10.1038/329506a0 |