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4GP3

The crystal structure of human fascin 1 K358A mutant

4GP3 の概要
エントリーDOI10.2210/pdb4gp3/pdb
関連するPDBエントリー4GOV 4GOY 4GP0
分子名称Fascin, BROMIDE ION, CHLORIDE ION, ... (5 entities in total)
機能のキーワードbeta-trefoil, actin bundling protein, cancer, metastasis, cell migration, actin-binding, phosphoprotein, protein binding, actin
由来する生物種Homo sapiens (human)
細胞内の位置Cytoplasm, cytoskeleton: Q16658
タンパク質・核酸の鎖数2
化学式量合計110929.69
構造登録者
Yang, S.Y.,Huang, F.K.,Huang, J.,Chen, S.,Jakoncic, J.,Leo-Macias, A.,Diaz-Avalos, R.,Chen, L.,Zhang, J.J.,Huang, X.Y. (登録日: 2012-08-20, 公開日: 2012-11-28, 最終更新日: 2023-09-13)
主引用文献Yang, S.,Huang, F.K.,Huang, J.,Chen, S.,Jakoncic, J.,Leo-Macias, A.,Diaz-Avalos, R.,Chen, L.,Zhang, J.J.,Huang, X.Y.
Molecular mechanism of fascin function in filopodial formation.
J.Biol.Chem., 288:274-284, 2013
Cited by
PubMed Abstract: Filopodia are cell surface protrusions that are essential for cell migration. This finger-like structure is supported by rigid tightly bundled actin filaments. The protein responsible for actin bundling in filopodia is fascin. However, the mechanism by which fascin functions in filopodial formation is not clear. Here we provide biochemical, cryo-electron tomographic, and x-ray crystal structural data demonstrating the unique structural characteristics of fascin. Systematic mutagenesis studies on 100 mutants of fascin indicate that there are two major actin-binding sites on fascin. Crystal structures of four fascin mutants reveal concerted conformational changes in fascin from inactive to active states in the process of actin bundling. Mutations in any one of the actin-binding sites impair the cellular function of fascin in filopodial formation. Altogether, our data reveal the molecular mechanism of fascin function in filopodial formation.
PubMed: 23184945
DOI: 10.1074/jbc.M112.427971
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.25 Å)
構造検証レポート
Validation report summary of 4gp3
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2026-02-04に公開中

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