1r5v
From Proteopedia
(Difference between revisions)
(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="450" color="white" frame="true" align="right" spinBox="true" | ||
- | 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== |
- | While in many cases the half-life of T cell receptor (TCR) binding to a | + | <StructureSection load='1r5v' size='340' side='right'caption='[[1r5v]], [[Resolution|resolution]] 2.50Å' scene=''> |
+ | == Structural highlights == | ||
+ | <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> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/HA22_MOUSE HA22_MOUSE] | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r5/1r5v_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1r5v" style="background-color:#fffaf0;"></div> | |
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- | + | ==See Also== | |
+ | *[[MHC 3D structures|MHC 3D structures]] | ||
+ | *[[MHC II 3D structures|MHC II 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Mus musculus]] | ||
+ | [[Category: Adams EJ]] | ||
+ | [[Category: Chow DC]] | ||
+ | [[Category: Davis MM]] | ||
+ | [[Category: Garcia KC]] | ||
+ | [[Category: He XL]] | ||
+ | [[Category: Krogsgaard M]] | ||
+ | [[Category: Prado N]] | ||
+ | [[Category: Wilson DB]] |
Current revision
Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T-cell activation
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Categories: Large Structures | Mus musculus | Adams EJ | Chow DC | Davis MM | Garcia KC | He XL | Krogsgaard M | Prado N | Wilson DB