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[[Image:1tvk.gif|left|200px]]
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{{STRUCTURE_1tvk|  PDB=1tvk  |  SCENE=  }}
'''The binding mode of epothilone A on a,b-tubulin by electron crystallography'''


==The binding mode of epothilone A on a,b-tubulin by electron crystallography==
<StructureSection load='1tvk' size='340' side='right'caption='[[1tvk]], [[Resolution|resolution]] 2.89&Aring;' 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]] 2.89&#8491;</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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1TVK is a [[Protein complex]] structure of sequences from [http://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].
</div>
<div class="pdbe-citations 1tvk" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15297674 15297674]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Cornett, B.]]
[[Category: Cornett B]]
[[Category: Downing, K H.]]
[[Category: Downing KH]]
[[Category: Krahn, J M.]]
[[Category: Krahn JM]]
[[Category: Li, H.]]
[[Category: Li H]]
[[Category: Nettles, J H.]]
[[Category: Nettles JH]]
[[Category: Snyder, J P.]]
[[Category: Snyder JP]]
[[Category: Epothilone]]
[[Category: Ligand interaction]]
[[Category: Taxol]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:25:25 2008''
Retrieved from "https://proteopedia.org/1tvk"