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2PBD

Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*

2PBD の概要
エントリーDOI10.2210/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
Ferron, F.,Rebowski, G.,Dominguez, R. (登録日: 2007-03-28, 公開日: 2007-11-13, 最終更新日: 2023-08-30)
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: 17914456
DOI: 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
Validation report summary of 2pbd
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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