Promiscuous binding of extracellular peptides to cell surface class I MHC protein
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 prom...
| Main Authors: | , , , , , , , , , , |
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| Other Authors: | |
| Format: | Article |
| Language: | en_US |
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National Academy of Sciences
2012
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| Online Access: | http://hdl.handle.net/1721.1/74019 https://orcid.org/0000-0002-5573-0137 https://orcid.org/0000-0002-5687-6154 |
| _version_ | 1826201917999546368 |
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| author | Eisen, Herman N. Hou, Xun Helen Shen, Chase Wang, Kaidi Tanguturi, Varsha Keelara Smith, Crysela Kozyrytska, Katerina Nambiar, Lakshmi McKinley, Carol A. Chen, Jianzhu Cohen, Richard J. |
| author2 | Harvard University--MIT Division of Health Sciences and Technology |
| author_facet | Harvard University--MIT Division of Health Sciences and Technology Eisen, Herman N. Hou, Xun Helen Shen, Chase Wang, Kaidi Tanguturi, Varsha Keelara Smith, Crysela Kozyrytska, Katerina Nambiar, Lakshmi McKinley, Carol A. Chen, Jianzhu Cohen, Richard J. |
| author_sort | Eisen, Herman N. |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T11:59:20Z |
| format | Article |
| id | mit-1721.1/74019 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T11:59:20Z |
| publishDate | 2012 |
| publisher | National Academy of Sciences |
| record_format | dspace |
| spelling | mit-1721.1/740192022-09-27T23:15:48Z Promiscuous binding of extracellular peptides to cell surface class I MHC protein Eisen, Herman N. Hou, Xun Helen Shen, Chase Wang, Kaidi Tanguturi, Varsha Keelara Smith, Crysela Kozyrytska, Katerina Nambiar, Lakshmi McKinley, Carol A. Chen, Jianzhu Cohen, Richard J. Harvard University--MIT Division of Health Sciences and Technology Massachusetts Institute of Technology. Department of Biology Koch Institute for Integrative Cancer Research at MIT Eisen, Herman N. Hou, Xun Helen Shen, Chase Wang, Kaidi Tanguturi, Varsha Keelara Smith, Crysela Kozyrytska, Katerina Nambiar, Lakshmi McKinley, Carol A. Chen, Jianzhu Cohen, Richard J. 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. Massachusetts Institute of Technology. Undergraduate Research Opportunities Program 2012-10-16T15:00:58Z 2012-10-16T15:00:58Z 2012-03 2012-01 Article http://purl.org/eprint/type/JournalArticle 0027-8424 1091-6490 http://hdl.handle.net/1721.1/74019 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 https://orcid.org/0000-0002-5573-0137 https://orcid.org/0000-0002-5687-6154 en_US http://dx.doi.org/10.1073/pnas.1201586109 Proceedings of the National Academy of Sciences Creative Commons Attribution http://creativecommons.org/licenses/by/2.5/ application/pdf National Academy of Sciences PNAS |
| spellingShingle | Eisen, Herman N. Hou, Xun Helen Shen, Chase Wang, Kaidi Tanguturi, Varsha Keelara Smith, Crysela Kozyrytska, Katerina Nambiar, Lakshmi McKinley, Carol A. Chen, Jianzhu Cohen, Richard J. Promiscuous binding of extracellular peptides to cell surface class I MHC protein |
| title | Promiscuous binding of extracellular peptides to cell surface class I MHC protein |
| title_full | Promiscuous binding of extracellular peptides to cell surface class I MHC protein |
| title_fullStr | Promiscuous binding of extracellular peptides to cell surface class I MHC protein |
| title_full_unstemmed | Promiscuous binding of extracellular peptides to cell surface class I MHC protein |
| title_short | Promiscuous binding of extracellular peptides to cell surface class I MHC protein |
| title_sort | promiscuous binding of extracellular peptides to cell surface class i mhc protein |
| url | http://hdl.handle.net/1721.1/74019 https://orcid.org/0000-0002-5573-0137 https://orcid.org/0000-0002-5687-6154 |
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