Modeling the interactions of a peptide-major histocompatibility class I ligand with its receptors. I. Recognition by two alpha beta T cell receptors.
A three-dimensional model of the complex between an Influenza Hemagglutinin peptide, Ha255-262, and its restricting element, the mouse major histocompatibility complex (MHC) class I molecule, Kk, was built by homology modeling and subsequently refined by simulated annealing and restrained molecular...
| Hlavní autoři: | , , , , , , |
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| Médium: | Journal article |
| Jazyk: | English |
| Vydáno: |
2000
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| _version_ | 1826272983621042176 |
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| author | Rognan, D Stryhn, A Fugger, L Lyngbaek, S Engberg, J Andersen, P Buus, S |
| author_facet | Rognan, D Stryhn, A Fugger, L Lyngbaek, S Engberg, J Andersen, P Buus, S |
| author_sort | Rognan, D |
| collection | OXFORD |
| description | A three-dimensional model of the complex between an Influenza Hemagglutinin peptide, Ha255-262, and its restricting element, the mouse major histocompatibility complex (MHC) class I molecule, Kk, was built by homology modeling and subsequently refined by simulated annealing and restrained molecular dynamics. Next, three-dimensional models of two different T cell receptors (TCRs) both specific for the Ha255-262/Kk complex were generated based on previously published TCR X-ray structures. Finally, guided by the recently published X-ray structures of ternary TCR/peptide/MHC-I complexes, the TCR models were successfully docked into the Ha255-262/Kk model. We have previously used a systematic and exhaustive panel of 144 single amino acid substituted analogs to analyze both MHC binding and T cell recognition of the parental viral peptide. This large body of experimental data was used to evaluate the models. They were found to account well for the experimentally obtained data, lending considerable support to the proposed models and suggesting a universal docking mode for alpha beta TCRs to MHC-peptide complexes. Such models may also be useful in guiding future rational experimentation. |
| first_indexed | 2024-03-06T22:21:12Z |
| format | Journal article |
| id | oxford-uuid:551cd3df-31a3-4818-8bd5-264053e001e2 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:21:12Z |
| publishDate | 2000 |
| record_format | dspace |
| spelling | oxford-uuid:551cd3df-31a3-4818-8bd5-264053e001e22022-03-26T16:41:57ZModeling the interactions of a peptide-major histocompatibility class I ligand with its receptors. I. Recognition by two alpha beta T cell receptors.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:551cd3df-31a3-4818-8bd5-264053e001e2EnglishSymplectic Elements at Oxford2000Rognan, DStryhn, AFugger, LLyngbaek, SEngberg, JAndersen, PBuus, SA three-dimensional model of the complex between an Influenza Hemagglutinin peptide, Ha255-262, and its restricting element, the mouse major histocompatibility complex (MHC) class I molecule, Kk, was built by homology modeling and subsequently refined by simulated annealing and restrained molecular dynamics. Next, three-dimensional models of two different T cell receptors (TCRs) both specific for the Ha255-262/Kk complex were generated based on previously published TCR X-ray structures. Finally, guided by the recently published X-ray structures of ternary TCR/peptide/MHC-I complexes, the TCR models were successfully docked into the Ha255-262/Kk model. We have previously used a systematic and exhaustive panel of 144 single amino acid substituted analogs to analyze both MHC binding and T cell recognition of the parental viral peptide. This large body of experimental data was used to evaluate the models. They were found to account well for the experimentally obtained data, lending considerable support to the proposed models and suggesting a universal docking mode for alpha beta TCRs to MHC-peptide complexes. Such models may also be useful in guiding future rational experimentation. |
| spellingShingle | Rognan, D Stryhn, A Fugger, L Lyngbaek, S Engberg, J Andersen, P Buus, S Modeling the interactions of a peptide-major histocompatibility class I ligand with its receptors. I. Recognition by two alpha beta T cell receptors. |
| title | Modeling the interactions of a peptide-major histocompatibility class I ligand with its receptors. I. Recognition by two alpha beta T cell receptors. |
| title_full | Modeling the interactions of a peptide-major histocompatibility class I ligand with its receptors. I. Recognition by two alpha beta T cell receptors. |
| title_fullStr | Modeling the interactions of a peptide-major histocompatibility class I ligand with its receptors. I. Recognition by two alpha beta T cell receptors. |
| title_full_unstemmed | Modeling the interactions of a peptide-major histocompatibility class I ligand with its receptors. I. Recognition by two alpha beta T cell receptors. |
| title_short | Modeling the interactions of a peptide-major histocompatibility class I ligand with its receptors. I. Recognition by two alpha beta T cell receptors. |
| title_sort | modeling the interactions of a peptide major histocompatibility class i ligand with its receptors i recognition by two alpha beta t cell receptors |
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