1r5v
From Proteopedia
(New page: 200px<br /><applet load="1r5v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r5v, resolution 2.5Å" /> '''Evidence that structu...) |
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| - | [[Image:1r5v.jpg|left|200px]]<br /><applet load="1r5v" size=" | + | [[Image:1r5v.jpg|left|200px]]<br /><applet load="1r5v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r5v, resolution 2.5Å" /> | caption="1r5v, resolution 2.5Å" /> | ||
'''Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T-cell activation'''<br /> | '''Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T-cell activation'''<br /> | ||
==Overview== | ==Overview== | ||
| - | While in many cases the half-life of T cell receptor (TCR) binding to a | + | 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== | ==About this Structure== | ||
| - | 1R5V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1R5V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R5V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Adams, E | + | [[Category: Adams, E J.]] |
| - | [[Category: Chow, D | + | [[Category: Chow, D C.]] |
| - | [[Category: Davis, M | + | [[Category: Davis, M M.]] |
| - | [[Category: Garcia, K | + | [[Category: Garcia, K C.]] |
| - | [[Category: He, X | + | [[Category: He, X L.]] |
[[Category: Krogsgaard, M.]] | [[Category: Krogsgaard, M.]] | ||
[[Category: Prado, N.]] | [[Category: Prado, N.]] | ||
| - | [[Category: Wilson, D | + | [[Category: Wilson, D B.]] |
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
[[Category: mhc class ii]] | [[Category: mhc class ii]] | ||
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[[Category: tcr]] | [[Category: tcr]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:25 2008'' |
Revision as of 12:47, 21 February 2008
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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
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