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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Bjorkman, P., Saper, M., Samraoui, B. et al. Structure of the human class I histocompatibility antigen, HLA-A2. Nature 329, 506–512 (1987). https://doi.org/10.1038/329506a0
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DOI: https://doi.org/10.1038/329506a0
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