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A hypothetical model of the foreign antigen binding site of Class II histocompatibility molecules

A hypothetical model of the foreign antigen binding site of Class II histocompatibility molecules Class II and class I histocompatibility molecules allow T cells to recognize 'processed' polypeptide antigens1–5. The two polypeptide chains of class II molecules, α and β, are each composed of two domains (for review see ref. 6); the N-terminal domains of each, α 1 and β 1, are highly polymorphic6–10 and appear responsible for binding peptides at what appears to be a single site11–13 and for being recognized by MHC-restricted antigen-specific T cells14,15. Recently, the three-dimensional structure of the foreign antigen binding site of a class I histocompatibility antigen has been described16,17. Because a crystal structure of a class II molecule is not available, we have sought evidence in class II molecules for the structural features observed in the class I binding site by comparing the patterns of conserved and polymorphic residues of twenty-six class I and fifty-four class II amino acid sequences. The hypothetical class II foreign-antigen binding site we present is consistent with mutation experiments18–28 and provides a structural framework for proposing peptide binding models to help understand recent peptide binding data11,29–33. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

A hypothetical model of the foreign antigen binding site of Class II histocompatibility molecules

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References (64)

Publisher
Springer Journals
Copyright
Copyright © 1988 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/332845a0
Publisher site
See Article on Publisher Site

Abstract

Class II and class I histocompatibility molecules allow T cells to recognize 'processed' polypeptide antigens1–5. The two polypeptide chains of class II molecules, α and β, are each composed of two domains (for review see ref. 6); the N-terminal domains of each, α 1 and β 1, are highly polymorphic6–10 and appear responsible for binding peptides at what appears to be a single site11–13 and for being recognized by MHC-restricted antigen-specific T cells14,15. Recently, the three-dimensional structure of the foreign antigen binding site of a class I histocompatibility antigen has been described16,17. Because a crystal structure of a class II molecule is not available, we have sought evidence in class II molecules for the structural features observed in the class I binding site by comparing the patterns of conserved and polymorphic residues of twenty-six class I and fifty-four class II amino acid sequences. The hypothetical class II foreign-antigen binding site we present is consistent with mutation experiments18–28 and provides a structural framework for proposing peptide binding models to help understand recent peptide binding data11,29–33.

Journal

Nature – Springer Journals

Published: Apr 28, 1988

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