Abstract
The class I histocompatibility antigen from human cell membranes (Ploegh et al., 1981) 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 (Bjorkman et al., 1987a). Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign antigens. Many residues critical for T-cell recognition of HLA are located in this site, in positions allowing them to serve as ligands to processed antigens (Bjorkman et al., 1987b).
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References
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Strominger, J.L. (1989). Structural and Functional Analysis of Human Class I and Class II Major Histocompatibility Complex Proteins, with Special Emphasis on Alloreactivity. In: Melchers, F., et al. Progress in Immunology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-83755-5_7
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DOI: https://doi.org/10.1007/978-3-642-83755-5_7
Publisher Name: Springer, Berlin, Heidelberg
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