3LUE

Model of alpha-actinin CH1 bound to F-actin

3LUE の概要

• エントリーDOI: 10.2210/pdb3lue/pdb
• EMDBエントリー: 5170
• 分子名称: Actin, cytoplasmic 1, Alpha-actinin-3 (2 entities in total)
• 機能のキーワード: calponin homology domains, acetylation, atp-binding, cytoplasm, cytoskeleton, methylation, nucleotide-binding, phosphoprotein, actin-binding, calcium, polymorphism, structural protein, deafness, disease mutation, dystonia
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 541231.77

構造登録者

Galkin, V.E.,Orlova, A.,Salmazo, A.,Djinovic-Carugo, K.,Egelman, E.H. (登録日: 2010-02-17, 公開日: 2010-04-28, 最終更新日: 2024-02-21)

主引用文献

Galkin, V.E.,Orlova, A.,Salmazo, A.,Djinovic-Carugo, K.,Egelman, E.H.
Opening of tandem calponin homology domains regulates their affinity for F-actin.
Nat.Struct.Mol.Biol., 17:614-616, 2010

PubMed Abstract: Many actin-binding proteins contain calponin homology (CH) domains, but the manner in which these domains interact with F-actin has been controversial. Crystal structures have shown the tandem CH domains of alpha-actinin to be in a compact, closed conformation, but the interpretations of complexes of such tandem CH domains with F-actin have been ambiguous. We show that the tandem CH domains of alpha-actinin bind F-actin in an open conformation, explaining mutations that cause human diseases and suggesting that the opening of these domains may be one of the main regulatory mechanisms for proteins with tandem CH domains.

PubMed: 20383143
DOI: 10.1038/nsmb.1789

実験手法

ELECTRON MICROSCOPY (15 Å)