1s1c
From Proteopedia
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Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI
Overview
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.
About this Structure
1S1C is a Protein complex structure of sequences from Homo sapiens with MG and GNP as ligands. Full crystallographic information is available from OCA.
Reference
Structural insights into the interaction of ROCKI with the switch regions of RhoA., Dvorsky R, Blumenstein L, Vetter IR, Ahmadian MR, J Biol Chem. 2004 Feb 20;279(8):7098-104. Epub 2003 Dec 2. PMID:14660612
Page seeded by OCA on Mon Nov 12 19:09:13 2007
Categories: Homo sapiens | Protein complex | Ahmadian, M.R. | Blumenstein, L. | Dvorsky, R. | Vetter, I.R. | GNP | MG | Coiled-coil | Gtpase | Rho kinase | Rock
