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PROSITE documentation PDOC50194

Filamin/ABP280 repeat profile


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 β-sandwich, formed by two β-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 β-sheet and that repeat 5 contributes to dimerisation to some extent [3,4].

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

Last update:

December 2001 / First entry.


Technical section

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

FILAMIN_REPEAT, PS50194; Filamin/ABP280 repeat profile  (MATRIX)


1AuthorsNoegel A.A. Rapp S. Lottspeich F. Schleicher M. Stewart M.
TitleThe 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.
SourceJ. Cell Biol. 109:607-618(1989).
PubMed ID2668299

2AuthorsFucini P. Renner C. Herberhold C. Noegel A.A. Holak T.A.
TitleThe repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold.
SourceNat. Struct. Biol. 4:223-230(1997).
PubMed ID9164464

3AuthorsMcCoy A.J. Fucini P. Noegel A.A. Stewart M.
TitleStructural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod.
SourceNat. Struct. Biol. 6:836-841(1999).
PubMed ID10467095

4AuthorsFucini P. Koppel B. Schleicher M. Lustig A. Holak T.A. Muller R. Stewart M. Noegel A.A.
TitleMolecular architecture of the rod domain of the Dictyostelium gelation factor (ABP120).
SourceJ. Mol. Biol. 291:1017-1023(1999).
PubMed ID10518939

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