{PDOC51859}
{PS51859; RHO_BD}
{BEGIN}
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* Rho-binding (RhoBD) domain profile *
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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/
ROKbeta/p160(ROCK) and  ROCKII/ROKalpha/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 alpha-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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: March 2018 / First entry.

[ 1] 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=12954645; DOI=10.1074/jbc.M306458200
[ 2] Dvorsky R., Blumenstein L., Vetter I.R., Ahmadian M.R.
     "Structural insights into the interaction of ROCKI with the switch
     regions of RhoA."
     J. Biol. Chem. 279:7098-7104(2004).
     PubMed=14660612; DOI=10.1074/jbc.M311911200

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