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2cik

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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, 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.
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.
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==Disease==
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Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142830 142830]], Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]], Spondyloarthropathy, susceptibility to, 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142830 142830]], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142830 142830]]
==About this Structure==
==About this Structure==
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[[Category: transmembrane]]
[[Category: transmembrane]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 18:10:05 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:15:54 2007''

Revision as of 19:09, 12 November 2007

Image:2cik.gif

2cik, resolution 1.75Å

Drag the structure with the mouse to rotate

INSIGHTS INTO CROSSREACTIVITY IN HUMAN ALLORECOGNITION: THE STRUCTURE OF HLA-B35011 PRESENTING AN EPITOPE DERIVED FROM CYTOCHROME P450.

Contents

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.

Disease

Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142830], Hypoproteinemia, hypercatabolic OMIM:[109700], Spondyloarthropathy, susceptibility to, 1 OMIM:[142830], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[142830]

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

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