{PDOC50194}
{PS50194; FILAMIN_REPEAT}
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* Filamin/ABP280 repeat profile *
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The many  different  actin cross-linking proteins share a common architecture,
consisting of  a  globular  actin-binding  domain and an extended rod. Whereas
their actin-binding   domains   consist   of  two  calponin  homology  domains
(see <PDOC50021>), their rods fall into three families.

The rod  domain  of  the  family  including  the Dictyostelium gelation factor
(ABP120) and  human  filamin  (ABP280) is constructed from tandem repeats of a
100-residue motif  that is glycine and proline rich [1]. The gelation factor's
rod contains  6  copies  of  the repeat, whereas filamin has a rod constructed
from 24  repeats.  The  resolution of the 3D structure of rod repeats from the
gelation factor  has shown that they consist of a beta-sandwich, formed by two
beta-sheets arranged  in  an immunoglobulin-like fold [2,3]. Because conserved
residues that  form  the  core  of  the  repeats are preserved in filamin, the
repeat structure   should   be   common   to   the  members  of  the  gelation
factor/filamin family.

The head to tail homodimerisation is crucial to the function of the ABP120 and
ABP280 proteins.  This  interaction involves a small portion at the distal end
of the  rod  domains.  For  the  gelation  factor  it  has been shown that the
carboxy-terminal repeat 6 dimerises through a double edge-to-edge extension of
the beta-sheet  and  that  repeat 5 contributes to dimerisation to some extent
[3,4].

The profile we developed covers the entire filamin/ABP280 repeat.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2001 / First entry.

[ 1] Noegel A.A., Rapp S., Lottspeich F., Schleicher M., Stewart M.
     "The Dictyostelium gelation factor shares a putative actin binding
     site with alpha-actinins and dystrophin and also has a rod domain
     containing six 100-residue motifs that appear to have a cross-beta
     conformation."
     J. Cell Biol. 109:607-618(1989).
     PubMed=2668299
[ 2] Fucini P., Renner C., Herberhold C., Noegel A.A., Holak T.A.
     "The repeating segments of the F-actin cross-linking gelation factor
     (ABP-120) have an immunoglobulin-like fold."
     Nat. Struct. Biol. 4:223-230(1997).
     PubMed=9164464
[ 3] McCoy A.J., Fucini P., Noegel A.A., Stewart M.
     "Structural basis for dimerization of the Dictyostelium gelation
     factor (ABP120) rod."
     Nat. Struct. Biol. 6:836-841(1999).
     PubMed=10467095; DOI=10.1038/12296
[ 4] Fucini P., Koppel B., Schleicher M., Lustig A., Holak T.A., Muller R.,
     Stewart M., Noegel A.A.
     "Molecular architecture of the rod domain of the Dictyostelium
     gelation factor (ABP120)."
     J. Mol. Biol. 291:1017-1023(1999).
     PubMed=10518939

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