1CXZ

CRYSTAL STRUCTURE OF HUMAN RHOA COMPLEXED WITH THE EFFECTOR DOMAIN OF THE PROTEIN KINASE PKN/PRK1

1CXZ の概要

• エントリーDOI: 10.2210/pdb1cxz/pdb
• 関連するPDBエントリー: 1A2B
• 分子名称: PROTEIN (HIS-TAGGED TRANSFORMING PROTEIN RHOA(0-181)), PROTEIN (PKN), MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: protein-protein complex, antiparallel coiled-coil, 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 : Q16512
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30971.42

構造登録者

Maesaki, R.,Ihara, K.,Shimizu, T.,Kuroda, S.,Kaibuchi, K.,Hakoshima, T. (登録日: 1999-08-31, 公開日: 1999-10-08, 最終更新日: 2024-05-22)

主引用文献

Maesaki, R.,Ihara, K.,Shimizu, T.,Kuroda, S.,Kaibuchi, K.,Hakoshima, T.
The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1.
Mol.Cell, 4:793-803, 1999

PubMed Abstract: The small G protein Rho has emerged as a key regulator of cellular events involving cytoskeletal reorganization. Here we report the 2.2 A crystal structure of RhoA bound to an effector domain of protein kinase PKN/PRK1. The structure reveals the antiparallel coiled-coil finger (ACC finger) fold of the effector domain that binds to the Rho specificity-determining regions containing switch I, beta strands B2 and B3, and the C-terminal alpha helix A5, predominantly by specific hydrogen bonds. The ACC finger fold is distinct from those for other small G proteins and provides evidence for the diverse ways of effector recognition. Sequence analysis based on the structure suggests that the ACC finger fold is widespread in Rho effector proteins.

PubMed: 10619026
DOI: 10.1016/S1097-2765(00)80389-5

実験手法

X-RAY DIFFRACTION (2.2 Å)