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-Structure paper
タイトル | The binding mode of epothilone A on alpha,beta-tubulin by electron crystallography. |
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ジャーナル・号・ページ | Science, Vol. 305, Issue 5685, Page 866-869, Year 2004 |
掲載日 | 2004年8月6日 |
著者 | James H Nettles / Huilin Li / Ben Cornett / Joseph M Krahn / James P Snyder / Kenneth H Downing / |
PubMed 要旨 | 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 ...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. |
リンク | Science / PubMed:15297674 |
手法 | EM (電子線結晶学) |
解像度 | 2.89 Å |
構造データ | PDB-1tvk: |
化合物 | ChemComp-GTP: ChemComp-GDP: ChemComp-EP: |
由来 |
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キーワード | CELL CYCLE / STRUCTURAL PROTEIN / epothilone; taxol; ligand interactions |