+検索条件
-Structure paper
| タイトル | The binding mode of epothilone A on alpha,beta-tubulin by electron crystallography. |
|---|---|
| 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 |
|
キーワード | CELL CYCLE / STRUCTURAL PROTEIN / epothilone; taxol; ligand interactions |
ムービー
コントローラー
構造ビューア
万見文献について



著者
リンク




キーワード