|PROSITE documentation PDOC50194 [for PROSITE entry PS50194]|
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 . 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.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Noegel A.A. Rapp S. Lottspeich F. Schleicher M. Stewart M.|
|Title||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.|
|Source||J. Cell Biol. 109:607-618(1989).|
|2||Authors||Fucini P. Renner C. Herberhold C. Noegel A.A. Holak T.A.|
|Title||The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold.|
|Source||Nat. Struct. Biol. 4:223-230(1997).|
|3||Authors||McCoy A.J. Fucini P. Noegel A.A. Stewart M.|
|Title||Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod.|
|Source||Nat. Struct. Biol. 6:836-841(1999).|
|4||Authors||Fucini P. Koppel B. Schleicher M. Lustig A. Holak T.A. Muller R. Stewart M. Noegel A.A.|
|Title||Molecular architecture of the rod domain of the Dictyostelium gelation factor (ABP120).|
|Source||J. Mol. Biol. 291:1017-1023(1999).|