Promiscuous binding of extracellular peptides to cell surface class I MHC protein.

Eisen, Herman N, Hou, Xun Helen, Shen, Chase, Wang, Kaidi, Tanguturi, Varsha Keelara, Smith, Crysela, Kozyrytska, Katerina, Nambiar, Lakshmi, McKinley, Carol A, Chen, Jianzhu, Cohen, Richard J (March 2012) Promiscuous binding of extracellular peptides to cell surface class I MHC protein. Proceedings of the National Academy of Sciences of USA, 109 (12). pp. 4580-4585. ISSN 0027-8424

URL: https://www.ncbi.nlm.nih.gov/pubmed/22403068
DOI: 10.1073/pnas.1201586109

Abstract

Algorithms derived from measurements of short-peptide (8-10 mers) binding to class I MHC proteins suggest that the binding groove of a class I MHC protein, such as K(b), can bind well over 1 million different peptides with significant affinity (<500 nM), a level of ligand-binding promiscuity approaching the level of heat shock protein binding of unfolded proteins. MHC proteins can, nevertheless, discriminate between similar peptides and bind many of them with high (nanomolar) affinity. Some insights into this high-promiscuity/high-affinity behavior and its impact on immunodominant peptides in T-cell responses to some infections and vaccination are suggested by results obtained here from testing a model developed to predict the number of cell surface peptide-MHC complexes that form on cells exposed to extracellular (exogenous) peptides.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
organs, tissues, organelles, cell types and functions > tissues types and functions > membranes
CSHL Authors:
Communities: CSHL labs > Hou lab
SWORD Depositor: CSHL Elements
Depositing User: CSHL Elements
Date: 20 March 2012
Date Deposited: 10 May 2022 14:05
Last Modified: 10 May 2022 14:05
PMCID: PMC3311345
URI: https://repository.cshl.edu/id/eprint/40604

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