2bnx
From Proteopedia
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CRYSTAL STRUCTURE OF THE DIMERIC REGULATORY DOMAIN OF MOUSE DIAPHANEOUS-RELATED FORMIN (DRF), MDIA1
Overview
Diaphanous-related formins (DRFs) regulate dynamics of unbranched actin, filaments during cell contraction and cytokinesis. DRFs are autoinhibited, through intramolecular binding of a Diaphanous autoinhibitory domain (DAD), to a conserved N-terminal regulatory element. Autoinhibition is relieved, through binding of the GTPase RhoA to the N-terminal element. We report, the crystal structure of the dimeric regulatory domain of the DRF, mDia1., Dimerization is mediated by an intertwined six-helix bundle, from which, extend two Diaphanous inhibitory domains (DIDs) composed of five armadillo, repeats. NMR and biochemical mapping indicate the RhoA and DAD binding, sites on the DID partially overlap, explaining activation of mDia1 by the, GTPase. RhoA binding also requires an additional structurally independent, segment adjacent to the DID. This regulatory construction, involving a, GTPase binding site spanning a flexibly tethered arm and the inhibitory, module, is observed in many autoinhibited effectors of Ras superfamily, GTPases, suggesting evolutionary pressure for this design.
About this Structure
2BNX is a Single protein structure of sequence from Mus musculus with CL as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis of Rho GTPase-mediated activation of the formin mDia1., Otomo T, Otomo C, Tomchick DR, Machius M, Rosen MK, Mol Cell. 2005 Apr 29;18(3):273-81. PMID:15866170
Page seeded by OCA on Wed Nov 21 08:51:04 2007
Categories: Mus musculus | Single protein | Machius, M. | Otomo, C. | Otomo, T. | Rosen, M. | Tomchick, D.R. | CL | Actin | Autoinhibition | Cytoskeleton | Nucleation | Structural protein
