1tvk | pdb_00001tvk

The binding mode of epothilone A on a,b-tubulin by electron crystallography

spinqualitylabelsall models 1tvk, resolution 2.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tvk is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron crystallography, Resolution 2.89Å Ligands: EP, GDP, GTP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tubulin 3D Structures

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