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


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.

SUBMITTER: Eisen HN 

PROVIDER: S-EPMC3311345 | biostudies-other | 2012 Mar

REPOSITORIES: biostudies-other

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

Eisen Herman N HN   Hou Xun Helen XH   Shen Chase C   Wang Kaidi K   Tanguturi Varsha Keelara VK   Smith Crysela C   Kozyrytska Katerina K   Nambiar Lakshmi L   McKinley Carol A CA   Chen Jianzhu J   Cohen Richard J RJ  

Proceedings of the National Academy of Sciences of the United States of America 20120307 12


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 insi  ...[more]

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