InterPro domain: IPR017868

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 IPR001715 ), their rods fall into three families.

The rod domain of the family including the Dictyostelium discoideum (Slime mould) gelation factor (ABP120) and human filamin (ABP280). It 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 , 2 ]. The repeat structure is common to the members of the gelation factor/filamin family.

This entry represents the entire filamin/ABP280 repeat.

1. The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold. Nat. Struct. Biol. 4, 223-30
2. Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod. Nat. Struct. Biol. 6, 836-41