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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Bibliographic Details
Published inNature (London) Vol. 329; no. 6139; p. 506
Main Authors Bjorkman, P J, Saper, M A, Samraoui, B, Bennett, W S, Strominger, J L, Wiley, D C
Format Journal Article
LanguageEnglish
Published England 08.10.1987
Subjects
Antigens - metabolism
beta 2-Microglobulin - metabolism
Binding Sites
Computer Graphics
Glycoproteins - metabolism
HLA Antigens - metabolism
HLA-A2 Antigen
Humans
Membrane Proteins - metabolism
Models, Molecular
Protein Binding
Protein Conformation
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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.
ISSN:0028-0836
DOI:10.1038/329506a0