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FH2 Domain
Class:Cytoskeletal modulation

No ImageFormin Homology-2 (FH2) domains are approximately 400 residues in length with an almost entirely alpha helical structure that dimerize in a head to tail fashion. The resulting symmetric homodimer forms a parallelogram like structure when viewed from the top. The homodimers interact by a lasso at the N-terminus of one monomer wrapping around a protuberance from the post subdomain at the C-terminus of the other monomer. This lasso and post interface is thought to mediate actin binding. A linker extends from each lasso and tethers the monomers to each other.

Structure Reference:
Xu, Y. et al. (2004) Cell 116(5), 711-723. PDB: 1UX4.

Domain binding and function:
The approximately 400 amino acid FH2 domain promotes filamentous actin growth by catalyzing the nucleation of actin chains. Interestingly, FH2 domains induce unbranched actin filaments unlike the Arp 2/3 complex which initiates branched actin filaments. FH2 domains are found in many proteins that are required in a variety of cytoskeletal dependent processes such as cellular polarity, morphogenesis, and cytokinesis.
Examples of Proteins:
mMDIA (AF051782)
DIAM1 (AB002379)
FHOS (AF113615)

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