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PMID: 3309677 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Structure of the human class I histocompatibility antigen, HLA-A2.

Nature ·Vol. 329 ·No. 6139 ·1987-00-00 ·Pages 506-12

Bjorkman PJ, Saper MA, Samraoui B, Bennett WS, Strominger JL, Wiley DC

Abstract

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.

MeSH Terms
Antigens/metabolism Binding Sites Computer Graphics Glycoproteins/metabolism HLA Antigens/metabolism HLA-A2 Antigen Humans Membrane Proteins/metabolism Models, Molecular Protein Binding Protein Conformation beta 2-Microglobulin/metabolism
Chemicals
Antigens Glycoproteins HLA Antigens HLA-A2 Antigen Membrane Proteins beta 2-Microglobulin
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Bjorkman P J
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.
Saper M A
Samraoui B
Bennett W S
Strominger J L
Wiley D C
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1987-00-00
Pages
506-12
Language
English
Region
England
NLM ID
0410462
Subset
IM
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