Promiscuous binding of extracellular peptides to cell surface class I MHC protein.
Identifieur interne : 000937 ( Ncbi/Merge ); précédent : 000936; suivant : 000938Promiscuous 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. CohenSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2012.
Descripteurs français
- KwdFr :
- Animaux, Antigènes d'histocompatibilité de classe I (génétique), Cinétique, Concentration inhibitrice 50, Dénaturation des protéines, Endocytose, Gènes MHC de classe I, Humains, Liaison aux protéines, Ligands, Lymphocytes T (immunologie), Membrane cellulaire (métabolisme), Modèles biologiques, Ovalbumine (), Peptides (), Pliage des protéines, Sites de fixation, Souris.
- MESH :
- génétique : Antigènes d'histocompatibilité de classe I.
- immunologie : Lymphocytes T.
- métabolisme : Membrane cellulaire.
- Animaux, Cinétique, Concentration inhibitrice 50, Dénaturation des protéines, Endocytose, Gènes MHC de classe I, Humains, Liaison aux protéines, Ligands, Modèles biologiques, Ovalbumine, Peptides, Pliage des protéines, Sites de fixation, Souris.
English descriptors
- KwdEn :
- Animals, Binding Sites, Cell Membrane (metabolism), Endocytosis, Genes, MHC Class I, Histocompatibility Antigens Class I (genetics), Humans, Inhibitory Concentration 50, Kinetics, Ligands, Mice, Models, Biological, Ovalbumin (chemistry), Peptides (chemistry), Protein Binding, Protein Denaturation, Protein Folding, T-Lymphocytes (immunology).
- MESH :
- chemical , chemistry : Ovalbumin, Peptides.
- chemical , genetics : Histocompatibility Antigens Class I.
- immunology : T-Lymphocytes.
- metabolism : Cell Membrane.
- Animals, Binding Sites, Endocytosis, Genes, MHC Class I, Humans, Inhibitory Concentration 50, Kinetics, Ligands, Mice, Models, Biological, Protein Binding, Protein Denaturation, Protein Folding.
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
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pubmed:22403068Le document en format XML
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<term>Dénaturation des protéines</term>
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<front><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>
</front>
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<Abstract><AbstractText>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.</AbstractText>
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<name sortKey="Hou, Xun Helen" sort="Hou, Xun Helen" uniqKey="Hou X" first="Xun Helen" last="Hou">Xun Helen Hou</name>
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<name sortKey="Smith, Crysela" sort="Smith, Crysela" uniqKey="Smith C" first="Crysela" last="Smith">Crysela Smith</name>
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