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1tvk
From Proteopedia
(New page: 200px<br /><applet load="1tvk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tvk, resolution 2.89Å" /> '''The binding mode of ...) |
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| - | [[Image:1tvk.gif|left|200px]]<br /><applet load="1tvk" size=" | + | [[Image:1tvk.gif|left|200px]]<br /><applet load="1tvk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tvk, resolution 2.89Å" /> | caption="1tvk, resolution 2.89Å" /> | ||
'''The binding mode of epothilone A on a,b-tubulin by electron crystallography'''<br /> | '''The binding mode of epothilone A on a,b-tubulin by electron crystallography'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of epothilone A, bound to alpha,beta-tubulin in | + | 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== | ==About this Structure== | ||
| - | 1TVK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with GDP, GTP and EP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1TVK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=GDP:'>GDP</scene>, <scene name='pdbligand=GTP:'>GTP</scene> and <scene name='pdbligand=EP:'>EP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TVK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Cornett, B.]] | [[Category: Cornett, B.]] | ||
| - | [[Category: Downing, K | + | [[Category: Downing, K H.]] |
| - | [[Category: Krahn, J | + | [[Category: Krahn, J M.]] |
[[Category: Li, H.]] | [[Category: Li, H.]] | ||
| - | [[Category: Nettles, J | + | [[Category: Nettles, J H.]] |
| - | [[Category: Snyder, J | + | [[Category: Snyder, J P.]] |
[[Category: EP]] | [[Category: EP]] | ||
[[Category: GDP]] | [[Category: GDP]] | ||
| Line 24: | Line 24: | ||
[[Category: epothilone; taxol; ligand interactions]] | [[Category: epothilone; taxol; ligand interactions]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:49 2008'' |
Revision as of 13:17, 21 February 2008
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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 with , and 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
Page seeded by OCA on Thu Feb 21 15:17:49 2008
