PROSITE documentation PDOC51859 [for PROSITE entry PS51859]

Rho-binding (RhoBD) domain profile

The Rho-ROCK pathway modulates the phosphorylation level of a variety of important signalling proteins and is thereby involved in miscellaneous cellular processes including cell migration, neurite outgrowth, and smooth muscle contraction. The enzyme activity of the two ROCK isoforms, ROCKI/ ROKβ/p160(ROCK) and ROCKII/ROKα/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 (see <PDOC51417>). ROCK proteins are composed of four domains: the N-terminal kinase domain (see <PDOC00100>), the long coiled-coil domain encompassing ~600 amino acid residues, the Rho-binding domain (RhoBD), and the C-terminal PH-like domain (see <PDOC50003>). The RhoBD is responsible for the recognition and binding of the active Rho proteins [1,2].

The RhoBD forms long consecutive α-helices dimerized in a parallel coiled-coil. The polypeptide chains of the middle region of the coiled-coil are flexible with poor inter-helical contacts between two chains (see <PDB:1UIX>) [1,2].

The profile we developed covers the entire RhoBD domain.