Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition

Small peptides, derived from endogenous proteins bind within the antigen binding groove created by the beta-pleated sheets and alpha helices of the alpha 1 and alpha 2 domains of the class I molecule of the major histocompatibility complex (MHC). However, the precise role of peptide in class I MHC c...

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Format: Online
Language:English
Published: The Rockefeller University Press 1992
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119441/
id pubmed-2119441
recordtype oai_dc
spelling pubmed-21194412008-04-16 Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition Articles Small peptides, derived from endogenous proteins bind within the antigen binding groove created by the beta-pleated sheets and alpha helices of the alpha 1 and alpha 2 domains of the class I molecule of the major histocompatibility complex (MHC). However, the precise role of peptide in class I MHC conformation remains unclear. Here, we have shown that, in at least some instances, changes induced in the MHC molecule by the binding of distinct peptides can be identified as specific alterations in serological epitopes expressed on the class I protein. The nature of specific peptides expressed by class I-bearing cells may, therefore, have a dramatic influence on T cell development, self-tolerance, and alloreactivity. The Rockefeller University Press 1992-12-01 /pmc/articles/PMC2119441/ /pubmed/1460430 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
title Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition
spellingShingle Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition
title_short Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition
title_full Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition
title_fullStr Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition
title_full_unstemmed Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition
title_sort peptide-induced conformational changes in class i heavy chains alter major histocompatibility complex recognition
description Small peptides, derived from endogenous proteins bind within the antigen binding groove created by the beta-pleated sheets and alpha helices of the alpha 1 and alpha 2 domains of the class I molecule of the major histocompatibility complex (MHC). However, the precise role of peptide in class I MHC conformation remains unclear. Here, we have shown that, in at least some instances, changes induced in the MHC molecule by the binding of distinct peptides can be identified as specific alterations in serological epitopes expressed on the class I protein. The nature of specific peptides expressed by class I-bearing cells may, therefore, have a dramatic influence on T cell development, self-tolerance, and alloreactivity.
publisher The Rockefeller University Press
publishDate 1992
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119441/
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