1tvk
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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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