2FXU
X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
Summary for 2FXU
| Entry DOI | 10.2210/pdb2fxu/pdb |
| Descriptor | Actin, alpha skeletal muscle, CALCIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | actin complexed to bistramide a, structural protein |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Cellular location | Cytoplasm, cytoskeleton: P68135 |
| Total number of polymer chains | 1 |
| Total formula weight | 43248.10 |
| Authors | Rizvi, S.A.,Tereshko, V.,Kossiakoff, A.A.,Kozmin, S.A. (deposition date: 2006-02-06, release date: 2006-03-07, Last modification date: 2023-08-30) |
| Primary citation | Rizvi, S.A.,Tereshko, V.,Kossiakoff, A.A.,Kozmin, S.A. Structure of bistramide a-actin complex at a 1.35 A resolution J.Am.Chem.Soc., 128:3882-3883, 2006 Cited by PubMed Abstract: Bistramide A is a highly potent antiproliferative marine natural product from Lissoclinum bistratum. We have previously established actin as the primary cellular receptor of bistramide A. We report herein the X-ray structure of bistramide A bound to monomeric actin at a resolution of 1.35 A. The most notable aspect of the bistramide A-actin structure is an extensive hydrogen-bonding network established upon a deep penetration of the central segment of bistramide A into the actin-binding cleft between subdomains 1 and 3. The structure presents the first insight into the observed ability of bistramide A to modulate G-actin polymerization. The structural information combined with our ability to chemically modify the bistramide framework provides the basis for rational development of a series of new synthetic analogues as useful probes for studying actin cytoskeleton and as potential therapeutic leads. PubMed: 16551075DOI: 10.1021/ja058319c PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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