1H67

NMR Structure of the CH Domain of Calponin

1H67 の概要

• エントリーDOI: 10.2210/pdb1h67/pdb
• NMR情報: BMRB: 4880
• 分子名称: CALPONIN ALPHA (1 entity in total)
• 機能のキーワード: cytoskeleton, calponin homology domain, actin binding
• 由来する生物種: GALLUS GALLUS (CHICKEN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12266.95

構造登録者

Bramham, J.,Smith, B.O.,Uhrin, D.,Barlow, P.N.,Winder, S.J. (登録日: 2001-06-07, 公開日: 2002-02-14, 最終更新日: 2024-05-15)

主引用文献

Bramham, J.,Hodgkinson, J.L.,Smith, B.O.,Uhrin, D.,Barlow, P.N.,Winder, S.J.
Solution Structure of the Calponin Ch Domain and Fitting to the 3D-Helical Reconstruction of F-Actin:Calponin.
Structure, 10:249-, 2002

PubMed Abstract: Calponin is involved in the regulation of contractility and organization of the actin cytoskeleton in smooth muscle cells. It is the archetypal member of the calponin homology (CH) domain family of actin binding proteins that includes cytoskeletal linkers such as alpha-actinin, spectrin, and dystrophin, and regulatory proteins including VAV, IQGAP, and calponin. We have determined the first structure of a CH domain from a single CH domain-containing protein, that of calponin, and have fitted the NMR-derived coordinates to the 3D-helical reconstruction of the F-actin:calponin complex using cryo-electron microscopy. The tertiary fold of this single CH domain is typical of, yet significantly different from, those of the CH domains that occur in tandem pairs to form high-affinity ABDs in other proteins. We thus provide a structural insight into the mode of interaction between F-actin and CH domain-containing proteins.

PubMed: 11839310
DOI: 10.1016/S0969-2126(02)00703-7

実験手法

SOLUTION NMR