1qrn

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(New page: 200px<br /> <applet load="1qrn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qrn, resolution 2.8&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1qrn.gif|left|200px]]<br /><applet load="1qrn" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1qrn" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1qrn, resolution 2.8&Aring;" />
caption="1qrn, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED WITH HLA-A2 BOUND TO ALTERED HTLV-1 TAX PEPTIDE P6A'''<br />
'''CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED WITH HLA-A2 BOUND TO ALTERED HTLV-1 TAX PEPTIDE P6A'''<br />
==Overview==
==Overview==
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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.
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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==
==Disease==
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==About this Structure==
==About this Structure==
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1QRN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QRN OCA].
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1QRN is a [http://en.wikipedia.org/wiki/Protein_complex 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==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Baker, B.M.]]
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[[Category: Baker, B M.]]
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[[Category: Biddison, W.E.]]
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[[Category: Biddison, W E.]]
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[[Category: Ding, Y.H.]]
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[[Category: Ding, Y H.]]
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[[Category: Garboczi, D.N.]]
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[[Category: Garboczi, D N.]]
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[[Category: Wiley, D.C.]]
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[[Category: Wiley, D C.]]
[[Category: hla-a2]]
[[Category: hla-a2]]
[[Category: htlv-1]]
[[Category: htlv-1]]
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[[Category: tcr]]
[[Category: tcr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:55:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:55 2008''

Revision as of 12:42, 21 February 2008


1qrn, resolution 2.8Å

Drag the structure with the mouse to rotate

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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