2PBD
Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*
2PBD の概要
| エントリーDOI | 10.2210/pdb2pbd/pdb |
| 関連するPDBエントリー | 2PAV |
| 分子名称 | Actin, alpha skeletal muscle, Profilin-1, Vasodilator-stimulated phosphoprotein, ... (6 entities in total) |
| 機能のキーワード | ternary complex; profilin; actin; vasp; poly-proline; loading poly-pro site; gab domain, structural protein |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Cytoplasm, cytoskeleton: P68135 P07737 Cytoplasm: P50552 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 61472.64 |
| 構造登録者 | |
| 主引用文献 | Ferron, F.,Rebowski, G.,Lee, S.H.,Dominguez, R. Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP Embo J., 26:4597-4606, 2007 Cited by PubMed Abstract: Cells sustain high rates of actin filament elongation by maintaining a large pool of actin monomers above the critical concentration for polymerization. Profilin-actin complexes constitute the largest fraction of polymerization-competent actin monomers. Filament elongation factors such as Ena/VASP and formin catalyze the transition of profilin-actin from the cellular pool onto the barbed end of growing filaments. The molecular bases of this process are poorly understood. Here we present structural and energetic evidence for two consecutive steps of the elongation mechanism: the recruitment of profilin-actin by the last poly-Pro segment of vasodilator-stimulated phosphoprotein (VASP) and the binding of profilin-actin simultaneously to this poly-Pro and to the G-actin-binding (GAB) domain of VASP. The actin monomer bound at the GAB domain is proposed to be in position to join the barbed end of the growing filament concurrently with the release of profilin. PubMed: 17914456DOI: 10.1038/sj.emboj.7601874 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.501 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






