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1tvk
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1tvk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tvk, resolution 2.89Å" /> '''The binding mode of ...) |
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| - | [[Image:1tvk.gif|left|200px]]<br /><applet load="1tvk" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1tvk, resolution 2.89Å" /> | ||
| - | '''The binding mode of epothilone A on a,b-tubulin by electron crystallography'''<br /> | ||
| - | == | + | ==The binding mode of epothilone A on a,b-tubulin by electron crystallography== |
| - | The structure of epothilone A, bound to alpha,beta-tubulin in | + | <StructureSection load='1tvk' size='340' side='right'caption='[[1tvk]], [[Resolution|resolution]] 2.89Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1tvk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TVK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 2.89Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EP:EPOTHILONE+A'>EP</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></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=1tvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tvk OCA], [https://pdbe.org/1tvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tvk RCSB], [https://www.ebi.ac.uk/pdbsum/1tvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tvk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TBA1D_BOVIN TBA1D_BOVIN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). | ||
| + | == 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/tv/1tvk_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1tvk ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The structure of epothilone A, bound to alpha,beta-tubulin in zinc-stabilized sheets, was determined by a combination of electron crystallography at 2.89 angstrom resolution and nuclear magnetic resonance-based conformational analysis. The complex explains both the broad-based epothilone structure-activity relationship and the known mutational resistance profile. Comparison with Taxol shows that the longstanding expectation of a common pharmacophore is not met, because each ligand exploits the tubulin-binding pocket in a unique and independent manner. | ||
| - | + | The binding mode of epothilone A on alpha,beta-tubulin by electron crystallography.,Nettles JH, Li H, Cornett B, Krahn JM, Snyder JP, Downing KH Science. 2004 Aug 6;305(5685):866-9. PMID:15297674<ref>PMID:15297674</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1tvk" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Tubulin 3D Structures|Tubulin 3D Structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bos taurus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cornett B]] | ||
| + | [[Category: Downing KH]] | ||
| + | [[Category: Krahn JM]] | ||
| + | [[Category: Li H]] | ||
| + | [[Category: Nettles JH]] | ||
| + | [[Category: Snyder JP]] | ||
Current revision
The binding mode of epothilone A on a,b-tubulin by electron crystallography
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Categories: Bos taurus | Large Structures | Cornett B | Downing KH | Krahn JM | Li H | Nettles JH | Snyder JP
