1UIX

Coiled-coil structure of the RhoA-binding domain in Rho-kinase

1UIX の概要

• エントリーDOI: 10.2210/pdb1uix/pdb
• 分子名称: Rho-associated kinase (2 entities in total)
• 機能のキーワード: coiled-coil, transferase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Cytoplasm: Q28021
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16111.83

構造登録者

Shimizu, T.,Ihara, K.,Maesaki, R.,Amano, M.,Kaibuchi, K.,Hakoshima, T. (登録日: 2003-07-23, 公開日: 2003-10-21, 最終更新日: 2024-11-20)

主引用文献

Shimizu, T.,Ihara, K.,Maesaki, R.,Amano, M.,Kaibuchi, K.,Hakoshima, T.
Parallel coiled-coil association of the RhoA-binding domain in Rho-kinase
J.Biol.Chem., 278:46046-46051, 2003

PubMed Abstract: Rho-kinase is a serine/threonine protein kinase that regulates cytoskeletal events in cells. The enzyme activity of Rho-kinase is auto-inhibited in the free state but is activated through direct binding to the small GTPase Rho in the GTP-bound form. The crystal structure of the Rho-binding domain (RhoBD) of Rho-kinase has been determined at 1.8-A resolution by the multi-wavelength anomalous dispersion technique. The structure shows that RhoBD dimerizes to form a parallel coiled-coil with long consecutive alpha-helices extended to approximately 97 A and suggests that free Rho-kinase can also form a dimer through parallel self-association. At the middle region of the coiled-coil, the polypeptide chains are flexible and display loose "knobs-into-holes" packing of the side chains from both chains. RhoBD residues that have been shown to be critical for Rho-binding are spread in the positively charged C-terminal region. The parallel coiled-coil structure of our Rho-kinase RhoBD in the free form is different from the anti-parallel coiled-coil structure of RhoBD of protein kinase N when complexed with RhoA. Implications derived from these structural studies in relation to the mechanism of Rho-kinase activation will be addressed with previously reported experimental data.

PubMed: 12954645
DOI: 10.1074/jbc.M306458200

実験手法

X-RAY DIFFRACTION (1.8 Å)