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TitleThe binding mode of epothilone A on alpha,beta-tubulin by electron crystallography.
Journal, issue, pagesScience, Vol. 305, Issue 5685, Page 866-869, Year 2004
Publish dateAug 6, 2004
AuthorsJames H Nettles / Huilin Li / Ben Cornett / Joseph M Krahn / James P Snyder / Kenneth H Downing /
PubMed AbstractThe 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 ...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.
External linksScience / PubMed:15297674
MethodsEM (electron crystallography)
Resolution2.89 Å
Structure data

PDB-1tvk:
The binding mode of epothilone A on a,b-tubulin by electron crystallography
Method: ELECTRON CRYSTALLOGRAPHY / Resolution: 2.89 Å

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-EP:
EPOTHILONE A

Source
  • bos taurus (cattle)
KeywordsCELL CYCLE / STRUCTURAL PROTEIN / epothilone; taxol; ligand interactions

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