1tvk: Difference between revisions
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|PDB= 1tvk |SIZE=350|CAPTION= <scene name='initialview01'>1tvk</scene>, resolution 2.89Å | |PDB= 1tvk |SIZE=350|CAPTION= <scene name='initialview01'>1tvk</scene>, resolution 2.89Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5 | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5'-TRIPHOSPHATE'>GTP</scene> and <scene name='pdbligand=EP:EPOTHILONE A'>EP</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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[[Category: epothilone; taxol; ligand interaction]] | [[Category: epothilone; taxol; ligand interaction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:47:31 2008'' | ||
Revision as of 14:47, 23 March 2008
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| , resolution 2.89Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The binding mode of epothilone A on a,b-tubulin by electron crystallography
OverviewOverview
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 StructureAbout this Structure
1TVK is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
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
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