2cik: Difference between revisions

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[[Image:2cik.jpg|left|200px]]<br /><applet load="2cik" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2cik.jpg|left|200px]]
caption="2cik, resolution 1.75&Aring;" />
 
'''INSIGHTS INTO CROSSREACTIVITY IN HUMAN ALLORECOGNITION: THE STRUCTURE OF HLA-B35011 PRESENTING AN EPITOPE DERIVED FROM CYTOCHROME P450.'''<br />
{{Structure
|PDB= 2cik |SIZE=350|CAPTION= <scene name='initialview01'>2cik</scene>, resolution 1.75&Aring;
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene>
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY=
|GENE=
}}
 
'''INSIGHTS INTO CROSSREACTIVITY IN HUMAN ALLORECOGNITION: THE STRUCTURE OF HLA-B35011 PRESENTING AN EPITOPE DERIVED FROM CYTOCHROME P450.'''
 


==Overview==
==Overview==
Line 10: Line 19:


==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 <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].  
2CIK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CIK OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17109469 17109469]
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:[http://www.ncbi.nlm.nih.gov/pubmed/17109469 17109469]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 40: Line 49:
[[Category: transmembrane]]
[[Category: transmembrane]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:49:03 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:15:52 2008''

Revision as of 14:15, 20 March 2008

File:2cik.jpg


Drag the structure with the mouse to rotate
2cik, resolution 1.75Å
Sites: AC1
Ligands: GOL
Coordinates: save as pdb, mmCIF, xml



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.

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. 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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