{PDOC51444}
{PS51444; FH2}
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* Formin homology-2 (FH2) domain profile *
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Formin proteins  participate  in a wide range of cytoskeletal processes in all
eukaryotes. They  promote nucleation and elongation of the actin filament, and
thus are  key  regulators for this process. The defining feature of formins is
a highly  conserved  ~400  residue region, the Formin Homology-2 (FH2) domain,
which forms  a head-to-tail ring-shaped dimer, and directly binds to the actin
filament at  its  barbed  end.  The  FH2  domain  catalyzes the nucleation and
elongation of  actin filament, preventing capping proteins from binding to the
barbed end [1,2].

The FH2  domain  is  almost  entirely alpha helical and can be subdivided into
five subdomains  with  somewhat  arbitrary  boundaries.  These  include  an N-
terminal "lasso",  a  "linker" segment, a globular "knob" subdomain, a coiled-
coil region,  and  a  carboxy-terminal "post" subdomain (see <PDB:1UX5>)>. The
dimer formation  is  mediated by unique interactions of "lasso" with "post" of
the partner FH2, exhibiting a closed ring structure [1,2].

The profile we developed covers the entire FH2 domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: March 2009 / First entry.

[ 1] Xu Y., Moseley J.B., Sagot I., Poy F., Pellman D., Goode B.L.,
     Eck M.J.
     "Crystal structures of a Formin Homology-2 domain reveal a tethered
     dimer architecture."
     Cell 116:711-723(2004).
     PubMed=15006353
[ 2] Yamashita M., Higashi T., Suetsugu S., Sato Y., Ikeda T.,
     Shirakawa R., Kita T., Takenawa T., Horiuchi H., Fukai S., Nureki O.
     "Crystal structure of human DAAM1 formin homology 2 domain."
     Genes Cells 12:1255-1265(2007).
     PubMed=17986009; DOI=10.1111/j.1365-2443.2007.01132.x

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