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PROSITE documentation PDOC51859

Rho-binding (RhoBD) domain profile





Description

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.

Last update:

March 2018 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

RHO_BD, PS51859; Rho-binding (RhoBD) domain profile  (MATRIX)


References

1AuthorsShimizu T. Ihara K. Maesaki R. Amano M. Kaibuchi K. Hakoshima T.
TitleParallel coiled-coil association of the RhoA-binding domain in Rho-kinase.
SourceJ. Biol. Chem. 278:46046-46051(2003).
PubMed ID12954645
DOI10.1074/jbc.M306458200

2AuthorsDvorsky R. Blumenstein L. Vetter I.R. Ahmadian M.R.
TitleStructural insights into the interaction of ROCKI with the switch regions of RhoA.
SourceJ. Biol. Chem. 279:7098-7104(2004).
PubMed ID14660612
DOI10.1074/jbc.M311911200



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