1r5v

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<StructureSection load='1r5v' size='340' side='right'caption='[[1r5v]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1r5v' size='340' side='right'caption='[[1r5v]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1r5v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R5V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1r5v]] is a 6 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R5V FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r5v OCA], [https://pdbe.org/1r5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r5v RCSB], [https://www.ebi.ac.uk/pdbsum/1r5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r5v ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r5v OCA], [https://pdbe.org/1r5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r5v RCSB], [https://www.ebi.ac.uk/pdbsum/1r5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r5v ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HB2I_MOUSE HB2I_MOUSE]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r5v ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r5v ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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<ref>PMID:14690592</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1r5v" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[MHC 3D structures|MHC 3D structures]]
*[[MHC 3D structures|MHC 3D structures]]
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== References ==
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*[[MHC II 3D structures|MHC II 3D structures]]
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Adams, E J]]
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[[Category: Adams EJ]]
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[[Category: Chow, D C]]
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[[Category: Chow DC]]
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[[Category: Davis, M M]]
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[[Category: Davis MM]]
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[[Category: Garcia, K C]]
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[[Category: Garcia KC]]
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[[Category: He, X L]]
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[[Category: He XL]]
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[[Category: Krogsgaard, M]]
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[[Category: Krogsgaard M]]
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[[Category: Prado, N]]
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[[Category: Prado N]]
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[[Category: Wilson, D B]]
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[[Category: Wilson DB]]
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[[Category: Mhc class ii]]
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[[Category: Signaling protein]]
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[[Category: Structural rearangement]]
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[[Category: Tcr]]
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Revision as of 06:10, 17 April 2024

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

PDB ID 1r5v

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