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2cik
From Proteopedia
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| - | [[Image:2cik.jpg|left|200px]]<br /><applet load="2cik" size=" | + | [[Image:2cik.jpg|left|200px]]<br /><applet load="2cik" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2cik, resolution 1.75Å" /> | caption="2cik, resolution 1.75Å" /> | ||
'''INSIGHTS INTO CROSSREACTIVITY IN HUMAN ALLORECOGNITION: THE STRUCTURE OF HLA-B35011 PRESENTING AN EPITOPE DERIVED FROM CYTOCHROME P450.'''<br /> | '''INSIGHTS INTO CROSSREACTIVITY IN HUMAN ALLORECOGNITION: THE STRUCTURE OF HLA-B35011 PRESENTING AN EPITOPE DERIVED FROM CYTOCHROME P450.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 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 <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CIK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:35:41 2008'' |
Revision as of 08:35, 3 February 2008
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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 as ligand. Known structural/functional Site: . 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 Sun Feb 3 10:35:41 2008
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
