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2cik
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Virus-specific T cell populations have been implicated in, allo-recognition. The subdominant T cell receptor JL12 recognizes both, HLA-B*0801 presenting the Epstein-Barr virus-derived peptide FLRGRAYGL and, also HLA-B*3501 presenting the cytochrome p450 self peptide KPIVVLHGY., This cross-reactivity could promote the rejection of HLA-B*3501-positive, cells in Epstein-Barr virus-exposed HLA-B*0801 recipients. LC13, the, dominant TCR against the HLA-B*0801:FLRGRAYGL complex, fails to recognize, HLA-B*3501:KPIVVLHGY. We report the 1.75-Angstrom resolution crystal, structure of the human allo-ligand HLA-B*3501:KPIVVLHGY. Similarities, between this structure and that of HLA-B*0801:FLRGRAYGL may facilitate, cross-recognition by JL12. Moreover, the elevated peptide position in, | + | Virus-specific T cell populations have been implicated in, allo-recognition. The subdominant T cell receptor JL12 recognizes both, HLA-B*0801 presenting the Epstein-Barr virus-derived peptide FLRGRAYGL and, also HLA-B*3501 presenting the cytochrome p450 self peptide KPIVVLHGY., This cross-reactivity could promote the rejection of HLA-B*3501-positive, cells in Epstein-Barr virus-exposed HLA-B*0801 recipients. LC13, the, dominant TCR against the HLA-B*0801:FLRGRAYGL complex, fails to recognize, HLA-B*3501:KPIVVLHGY. We report the 1.75-Angstrom resolution crystal, structure of the human allo-ligand HLA-B*3501:KPIVVLHGY. Similarities, between this structure and that of HLA-B*0801:FLRGRAYGL may facilitate, cross-recognition by JL12. Moreover, the elevated peptide position in, HLA-B*3501:KPIVVLHGY would provide steric hindrance to LC13, preventing it, from interacting in the manner in which it interacts with, HLA-B*0801:FLRGRAYGL. These findings are relevant to understanding the, basis of T cell cross-reactivity in allo-recognition, optimal transplant, donor-recipient matching and developing specific molecular inhibitors of, allo-recognition. |
==About this Structure== | ==About this Structure== | ||
| - | 2CIK is a | + | 2CIK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CIK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:16:30 2007'' |
Revision as of 13:11, 5 November 2007
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INSIGHTS INTO CROSSREACTIVITY IN HUMAN ALLORECOGNITION: THE STRUCTURE OF HLA-B35011 PRESENTING AN EPITOPE DERIVED FROM CYTOCHROME P450.
Overview
Virus-specific T cell populations have been implicated in, allo-recognition. The subdominant T cell receptor JL12 recognizes both, HLA-B*0801 presenting the Epstein-Barr virus-derived peptide FLRGRAYGL and, also HLA-B*3501 presenting the cytochrome p450 self peptide KPIVVLHGY., This cross-reactivity could promote the rejection of HLA-B*3501-positive, cells in Epstein-Barr virus-exposed HLA-B*0801 recipients. LC13, the, dominant TCR against the HLA-B*0801:FLRGRAYGL complex, fails to recognize, HLA-B*3501:KPIVVLHGY. We report the 1.75-Angstrom resolution crystal, structure of the human allo-ligand HLA-B*3501:KPIVVLHGY. Similarities, between this structure and that of HLA-B*0801:FLRGRAYGL may facilitate, cross-recognition by JL12. Moreover, the elevated peptide position in, HLA-B*3501:KPIVVLHGY would provide steric hindrance to LC13, preventing it, from interacting in the manner in which it interacts with, HLA-B*0801:FLRGRAYGL. These findings are relevant to understanding the, basis of T cell cross-reactivity in allo-recognition, optimal transplant, donor-recipient matching and developing specific molecular inhibitors of, allo-recognition.
About this Structure
2CIK is a Protein complex structure of sequences from Homo sapiens with GOL as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
The structure of the human allo-ligand HLA-B*3501 in complex with a cytochrome p450 peptide: steric hindrance influences TCR allo-recognition., Hourigan CS, Harkiolaki M, Peterson NA, Bell JI, Jones EY, O'Callaghan CA, Eur J Immunol. 2006 Dec;36(12):3288-93. PMID:17109469
Page seeded by OCA on Mon Nov 5 15:16:30 2007
Categories: Homo sapiens | Protein complex | Bell, J.I. | Callaghan, C.A.O. | Harkiolaki, M. | Hourigan, C.S. | Jones, E.Y. | Peterson, N.A. | GOL | Allo-ligand | Antigen/peptide complex | Ebv | Glycoprotein | Hla | Hla-b3501 | Human | Immune response | Immunoglobulin domain | Major histocompatibility antigen | Membrane | Mhc | Mhc i | Polymorphism | Pyrrolidone carboxylic acid | Transmembrane
