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dc.contributor.authorEisen, Herman N.
dc.contributor.authorHou, Xun Helen
dc.contributor.authorShen, Chase
dc.contributor.authorWang, Kaidi
dc.contributor.authorTanguturi, Varsha Keelara
dc.contributor.authorSmith, Crysela
dc.contributor.authorKozyrytska, Katerina
dc.contributor.authorNambiar, Lakshmi
dc.contributor.authorMcKinley, Carol A.
dc.contributor.authorChen, Jianzhu
dc.contributor.authorCohen, Richard J.
dc.date.accessioned2012-11-07T20:11:00Z
dc.date.available2012-11-07T20:11:00Z
dc.date.issued2012-03
dc.date.submitted2012-01
dc.identifier.issn0027-8424
dc.identifier.issn1091-6490
dc.identifier.urihttp://hdl.handle.net/1721.1/74590
dc.description.abstractAlgorithms 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.en_US
dc.description.sponsorshipMassachusetts Institute of Technology. Undergraduate Research Opportunities Programen_US
dc.language.isoen_US
dc.publisherNational Academy of Sciencesen_US
dc.relation.isversionofhttp://dx.doi.org/10.1073/pnas.1201586109en_US
dc.sourcePNASen_US
dc.titlePromiscuous binding of extracellular peptides to cell surface class I MHC proteinen_US
dc.typeArticleen_US
dc.identifier.citationEisen, 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 Sciencesen_US
dc.contributor.departmentHarvard University--MIT Division of Health Sciences and Technologyen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.departmentKoch Institute for Integrative Cancer Research at MITen_US
dc.contributor.mitauthorEisen, Herman N.
dc.contributor.mitauthorHou, Xun Helen
dc.contributor.mitauthorShen, Chase
dc.contributor.mitauthorWang, Kaidi
dc.contributor.mitauthorTanguturi, Varsha Keelara
dc.contributor.mitauthorSmith, Crysela
dc.contributor.mitauthorKozyrytska, Katerina
dc.contributor.mitauthorNambiar, Lakshmi
dc.contributor.mitauthorMcKinley, Carol A.
dc.contributor.mitauthorChen, Jianzhu
dc.contributor.mitauthorCohen, Richard J.
dc.relation.journalProceedings of the National Academy of Sciencesen_US
dc.eprint.versionFinal published versionen_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsEisen, H. N.; Hou, X. H.; Shen, C.; Wang, K.; Tanguturi, V. K.; Smith, C.; Kozyrytska, K.; Nambiar, L.; McKinley, C. A.; Chen, J.; Cohen, R. J.en
dc.identifier.orcidhttps://orcid.org/0000-0002-5573-0137
dc.identifier.orcidhttps://orcid.org/0000-0002-5687-6154
mit.licensePUBLISHER_POLICYen_US


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