2cik: Difference between revisions
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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. | ||
==Disease== | |||
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]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:15:54 2007'' | ||
