1QQV
SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN
1QQV の概要
エントリーDOI | 10.2210/pdb1qqv/pdb |
NMR情報 | BMRB: 4428 |
分子名称 | VILLIN HEADPIECE DOMAIN (1 entity in total) |
機能のキーワード | f-actin binding domain, salt-bridge, structural protein |
由来する生物種 | Gallus gallus (chicken) |
細胞内の位置 | Cytoplasm, cytoskeleton: P02640 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 7611.66 |
構造登録者 | Vardar, D.,Buckley, D.A.,Frank, B.S.,McKnight, C.J. (登録日: 1999-06-08, 公開日: 1999-12-29, 最終更新日: 2024-05-22) |
主引用文献 | Vardar, D.,Buckley, D.A.,Frank, B.S.,McKnight, C.J. NMR structure of an F-actin-binding "headpiece" motif from villin. J.Mol.Biol., 294:1299-1310, 1999 Cited by PubMed Abstract: A growing family of F-actin-bundling proteins harbors a modular F-actin-binding headpiece domain at the C terminus. Headpiece provides one of the two F-actin-binding sites essential for filament bundling. Here, we report the first structure of a functional headpiece domain. The NMR structure of chicken villin headpiece (HP67) reveals two subdomains that share a tightly packed hydrophobic core. The N-terminal subdomain contains bends, turns, and a four-residue alpha-helix as well as a buried histidine residue that imparts a pH-dependent folding. The C-terminal subdomain is composed of three alpha-helices and its folding is pH-independent. Two residues previously implicated in F-actin-binding form a buried salt-bridge between the N and C-terminal subdomains. The rest of the identified actin-binding residues are solvent-exposed and map onto a unique F-actin-binding surface. PubMed: 10600386DOI: 10.1006/jmbi.1999.3321 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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