1r5v

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[[Image:1r5v.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1r5v", creates the "Structure Box" on the page.
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{{STRUCTURE_1r5v| PDB=1r5v | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r5v OCA], [http://www.ebi.ac.uk/pdbsum/1r5v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r5v RCSB]</span>
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'''Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T-cell activation'''
'''Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T-cell activation'''
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[[Category: Prado, N.]]
[[Category: Prado, N.]]
[[Category: Wilson, D B.]]
[[Category: Wilson, D B.]]
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[[Category: crystal structure]]
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[[Category: Crystal structure]]
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[[Category: mhc class ii]]
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[[Category: Mhc class ii]]
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[[Category: structural rearangement]]
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[[Category: Structural rearangement]]
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[[Category: tcr]]
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[[Category: Tcr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:07:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:23:39 2008''
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Revision as of 04:07, 3 May 2008

Template:STRUCTURE 1r5v

Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T-cell activation


Overview

While in many cases the half-life of T cell receptor (TCR) binding to a particular ligand is a good predictor of activation potential, numerous exceptions suggest that other physical parameter(s) must also play a role. Accordingly, we analyzed the thermodynamics of TCR binding to a series of peptide-MHC ligands, three of which are more stimulatory than their stability of binding would predict. Strikingly, we find that during TCR binding these outliers show anomalously large changes in heat capacity, an indicator of conformational change or flexibility in a binding interaction. By combining the values for heat capacity (DeltaCp) and the half-life of TCR binding (t(1/2)), we find that we can accurately predict the degree of T cell stimulation. Structural analysis shows significant changes in the central TCR contact residue of the peptide-MHC, indicating that structural rearrangements within the TCR-peptide-MHC interface can contribute to T cell activation.

About this Structure

1R5V is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation., Krogsgaard M, Prado N, Adams EJ, He XL, Chow DC, Wilson DB, Garcia KC, Davis MM, Mol Cell. 2003 Dec;12(6):1367-78. PMID:14690592 Page seeded by OCA on Sat May 3 07:07:08 2008

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