2cik | pdb_00002cik

File:2cik.gif

spinqualitylabelsall models 2cik, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

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, ... [(full description)]

About this Structure

2CIK is a [Protein complex] structure of sequences from [Homo sapiens] with GOL as [ligand]. 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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