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

Identifieur interne : 002220 ( Main/Exploration ); précédent : 002219; suivant : 002221

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

Auteurs : Herman N. Eisen [États-Unis] ; Xun Helen Hou ; Chase Shen ; Kaidi Wang ; Varsha Keelara Tanguturi ; Crysela Smith ; Katerina Kozyrytska ; Lakshmi Nambiar ; Carol A. Mckinley ; Jianzhu Chen ; Richard J. Cohen

Source :

RBID : pubmed:22403068

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English descriptors

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.

DOI: 10.1073/pnas.1201586109
PubMed: 22403068


Affiliations:


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Le document en format XML

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<name sortKey="Kozyrytska, Katerina" sort="Kozyrytska, Katerina" uniqKey="Kozyrytska K" first="Katerina" last="Kozyrytska">Katerina Kozyrytska</name>
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<term>Binding Sites</term>
<term>Cell Membrane (metabolism)</term>
<term>Endocytosis</term>
<term>Genes, MHC Class I</term>
<term>Histocompatibility Antigens Class I (genetics)</term>
<term>Humans</term>
<term>Inhibitory Concentration 50</term>
<term>Kinetics</term>
<term>Ligands</term>
<term>Mice</term>
<term>Models, Biological</term>
<term>Ovalbumin (chemistry)</term>
<term>Peptides (chemistry)</term>
<term>Protein Binding</term>
<term>Protein Denaturation</term>
<term>Protein Folding</term>
<term>T-Lymphocytes (immunology)</term>
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<term>Animaux</term>
<term>Antigènes d'histocompatibilité de classe I (génétique)</term>
<term>Cinétique</term>
<term>Concentration inhibitrice 50</term>
<term>Dénaturation des protéines</term>
<term>Endocytose</term>
<term>Gènes MHC de classe I</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Ligands</term>
<term>Lymphocytes T (immunologie)</term>
<term>Membrane cellulaire (métabolisme)</term>
<term>Modèles biologiques</term>
<term>Ovalbumine ()</term>
<term>Peptides ()</term>
<term>Pliage des protéines</term>
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<term>Ovalbumin</term>
<term>Peptides</term>
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<term>Histocompatibility Antigens Class I</term>
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<term>Antigènes d'histocompatibilité de classe I</term>
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<term>Lymphocytes T</term>
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<keywords scheme="MESH" qualifier="immunology" xml:lang="en">
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<term>Animals</term>
<term>Binding Sites</term>
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<term>Genes, MHC Class I</term>
<term>Humans</term>
<term>Inhibitory Concentration 50</term>
<term>Kinetics</term>
<term>Ligands</term>
<term>Mice</term>
<term>Models, Biological</term>
<term>Protein Binding</term>
<term>Protein Denaturation</term>
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<term>Cinétique</term>
<term>Concentration inhibitrice 50</term>
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<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Ligands</term>
<term>Modèles biologiques</term>
<term>Ovalbumine</term>
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<div type="abstract" xml:lang="en">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.</div>
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