1tvk | pdb_00001tvk
The binding mode of epothilone A on a,b-tubulin by electron crystallography
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Overview
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
1TVK is a Protein complex structure of sequences from Bos taurus with GDP, GTP and EP as ligands. Full crystallographic information is available from OCA.
Reference
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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