1UIX

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

Summary for 1UIX

• Entry DOI: 10.2210/pdb1uix/pdb
• Descriptor: Rho-associated kinase (2 entities in total)
• Functional Keywords: coiled-coil, transferase
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm: Q28021
• Total number of polymer chains: 2
• Total formula weight: 16111.83

Authors

Shimizu, T.,Ihara, K.,Maesaki, R.,Amano, M.,Kaibuchi, K.,Hakoshima, T. (deposition date: 2003-07-23, release date: 2003-10-21, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)