1tvk: Difference between revisions

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[[Image:1tvk.gif|left|200px]]
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[[Image:1tvk.png|left|200px]]


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{{STRUCTURE_1tvk|  PDB=1tvk  |  SCENE=  }}  
{{STRUCTURE_1tvk|  PDB=1tvk  |  SCENE=  }}  


'''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===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15297674}}


==About this Structure==
==About this Structure==
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[[Category: Ligand interaction]]
[[Category: Ligand interaction]]
[[Category: Taxol]]
[[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 Sun Jul 27 20:30:38 2008''

Revision as of 17:30, 27 July 2008

File:1tvk.png

Template:STRUCTURE 1tvk

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

Template:ABSTRACT PUBMED 15297674

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

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