 FH2 Domain | |
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| Class:Cytoskeletal modulation | |
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Structure:
 Formin 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.
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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.
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Examples of Proteins:
mMDIA (AF051782)
DIAM1 (AB002379)
FHOS (AF113615)
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Referenced in part on Cell Signaling Technology Website, Reference Section on Protein Domains. We gratefully acknowledge the following contributors:
Piers Nash1, Dan Lin3, Kathleen Binns2, Clark Wells2, Rob Ingham2, Terry Kubiseski2, Bernard Liu1, Matt Smith2,3, Ivan Blasutig2,3, Maria Sierra1, Caesar Lim2,3, Michael Arc1, Jim Fawcett2 and Tony Pawson2,3.
1. Ben May Institute for Cancer Research, The University of Chicago, Chicago, Illinois, 60637, USA
2. Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, M5G 1X5, Canada
3. Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada
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