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1tvk
From Proteopedia
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[[Image:1tvk.gif|left|200px]] | [[Image:1tvk.gif|left|200px]] | ||
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'''The binding mode of epothilone A on a,b-tubulin by electron crystallography''' | '''The binding mode of epothilone A on a,b-tubulin by electron crystallography''' | ||
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[[Category: Nettles, J H.]] | [[Category: Nettles, J H.]] | ||
[[Category: Snyder, J P.]] | [[Category: Snyder, J P.]] | ||
| - | [[Category: | + | [[Category: Epothilone]] |
| - | [[Category: | + | [[Category: Ligand interaction]] |
| - | [[Category: | + | [[Category: Taxol]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:25:25 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:25, 3 May 2008
The binding mode of epothilone A on a,b-tubulin by electron crystallography
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. 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 Page seeded by OCA on Sat May 3 10:25:25 2008
