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

PJ Bjorkman, MA Saper, B Samraoui, WS Bennett… - Nature, 1987 - nature.com
PJ Bjorkman, MA Saper, B Samraoui, WS Bennett, JL Strominger, DC Wiley
Nature, 1987nature.com
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 β-strands topped by α-helices. A large groove between the α-
helices provides a binding site for processed foreign antigens. An unknown'antigen'is found
in this site in crystals of purified HLA-A2.
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 β-strands topped by α-helices. A large groove between the α-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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