1S1C

Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI

1S1C の概要

• エントリーDOI: 10.2210/pdb1s1c/pdb
• 分子名称: Transforming protein RhoA, Rho-associated, coiled-coil containing protein kinase 1, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: coiled-coil, gtpase, rho kinase, rock, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane; Lipid-anchor; Cytoplasmic side: P61586; Cytoplasm: Q13464
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 59211.46

構造登録者

Dvorsky, R.,Blumenstein, L.,Vetter, I.R.,Ahmadian, M.R. (登録日: 2004-01-06, 公開日: 2004-02-10, 最終更新日: 2024-02-14)

主引用文献

Dvorsky, R.,Blumenstein, L.,Vetter, I.R.,Ahmadian, M.R.
Structural Insights into the Interaction of ROCKI with the Switch Regions of RhoA.
J.Biol.Chem., 279:7098-7104, 2004

PubMed Abstract: The Rho-ROCK pathway modulates the phosphorylation level of a variety of important signaling proteins and is thereby involved in miscellaneous cellular processes including cell migration, neurite outgrowth, and smooth muscle contraction. The observation of the involvement of the Rho-ROCK pathway in tumor invasion and in diseases such as hypertension and bronchial asthma makes it an interesting target for drug development. We herein present the crystal structure of the complex between active RhoA and the Rho-binding domain of ROCKI. The Rho-binding domain structure forms a parallel alpha-helical coiled-coil dimer and, in contrast to the published Rho-protein kinase N structure, binds exclusively to the switch I and II regions of the guanosine 5'-(beta,gamma-imido)triphosphate-bound RhoA. The switch regions of two different RhoA molecules form a predominantly hydrophobic patch, which is complementarily bound by two identical short helices of 13 residues (amino acids 998-1010). The identified ROCK-binding site of RhoA strikingly supports the assumption of a common consensus-binding site for effector recognition.

PubMed: 14660612
DOI: 10.1074/jbc.M311911200

実験手法

X-RAY DIFFRACTION (2.6 Å)