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1tvk

From Proteopedia

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{{STRUCTURE_1tvk| PDB=1tvk | SCENE= }}
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'''The binding mode of epothilone A on a,b-tubulin by electron crystallography'''
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===The binding mode of epothilone A on a,b-tubulin by electron crystallography===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 15297674 is the PubMed ID number.
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:25:25 2008''
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''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

Image: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

Page seeded by OCA on Sun Jul 27 20:30:38 2008

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