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. 1987 Oct;329(6139):506-12.
doi: 10.1038/329506a0.

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

P J Bjorkman  1 , M A Saper, B Samraoui, W S Bennett, J L Strominger, D C Wiley
Affiliations

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

P J Bjorkman et al. Nature. 1987 Oct.

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.

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