1qrn
From Proteopedia
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| - | [[Image:1qrn.gif|left|200px]] | + | [[Image:1qrn.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED WITH HLA-A2 BOUND TO ALTERED HTLV-1 TAX PEPTIDE P6A''' | + | {{Structure |
| + | |PDB= 1qrn |SIZE=350|CAPTION= <scene name='initialview01'>1qrn</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED WITH HLA-A2 BOUND TO ALTERED HTLV-1 TAX PEPTIDE P6A''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QRN is a [ | + | 1QRN 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=1QRN OCA]. |
==Reference== | ==Reference== | ||
| - | Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical., Ding YH, Baker BM, Garboczi DN, Biddison WE, Wiley DC, Immunity. 1999 Jul;11(1):45-56. PMID:[http:// | + | Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical., Ding YH, Baker BM, Garboczi DN, Biddison WE, Wiley DC, Immunity. 1999 Jul;11(1):45-56. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10435578 10435578] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: tcr]] | [[Category: tcr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:41:47 2008'' |
Revision as of 11:41, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED WITH HLA-A2 BOUND TO ALTERED HTLV-1 TAX PEPTIDE P6A
Contents |
Overview
The interactions of three singly substituted peptide variants of the HTLV-1 Tax peptide bound to HLA-A2 with the A6 T cell receptor have been studied using T cell assays, kinetic and thermodynamic measurements, and X-ray crystallography. The three peptide/MHC ligands include weak agonists and antagonists with different affinities for TCR. The three-dimensional structures of the three A6-TCR/peptide/HLA-A2 complexes are remarkably similar to each other and to the wild-type agonist complex, with minor adjustments at the interface to accommodate the peptide substitutions (P6A, V7R, and Y8A). The lack of correlation between structural changes and the type of T cell signals induced provides direct evidence that different signals are not generated by different ligand-induced conformational changes in the alphabeta TCR.
Disease
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142800], Ankylosing spondylitis, susceptibility to, 1 OMIM:[142800], Hypoproteinemia, hypercatabolic OMIM:[109700], Stevens-Johnson syndrome, susceptibility to OMIM:[142800]
About this Structure
1QRN is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical., Ding YH, Baker BM, Garboczi DN, Biddison WE, Wiley DC, Immunity. 1999 Jul;11(1):45-56. PMID:10435578
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