Promiscuous binding of extracellular peptides to cell surface class I MHC protein
Name
Eisen-2012-Promiscuous binding.pdf
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805.45 KB
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Checksum (MD5)
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Author(s)
Eisen, Herman N.
Hou, Xun Helen
Shen, Chase
Wang, Kaidi
Tanguturi, Varsha Keelara
Smith, Crysela
Kozyrytska, Katerina
Nambiar, Lakshmi
McKinley, Carol A.
Chen, Jianzhu
Date Issued
March 2012
Journal
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Citation
Eisen, H. N. et al. “Promiscuous Binding of Extracellular Peptides to Cell Surface Class I MHC Protein.” Proceedings of the National Academy of Sciences 109.12 (2012): 4580–4585. ©2012 by the National Academy of Sciences
Version
Final published version
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[superscript 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.
MIT Department
Harvard University--MIT Division of Health Sciences and Technology
Massachusetts Institute of Technology. Department of Biology
Koch Institute for Integrative Cancer Research at MIT
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1073/pnas.1201586109
