4YDH
The structure of human FMNL1 N-terminal domains bound to Cdc42
Summary for 4YDH
| Entry DOI | 10.2210/pdb4ydh/pdb |
| Related | 4YC7 |
| Descriptor | Formin-like protein 1, Cell division control protein 42 homolog, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | actin cytoskeleton, gtpase, formin, signaling protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 139775.12 |
| Authors | |
| Primary citation | Kuhn, S.,Erdmann, C.,Kage, F.,Block, J.,Schwenkmezger, L.,Steffen, A.,Rottner, K.,Geyer, M. The structure of FMNL2-Cdc42 yields insights into the mechanism of lamellipodia and filopodia formation. Nat Commun, 6:7088-7088, 2015 Cited by PubMed Abstract: Formins are actin polymerization factors that elongate unbranched actin filaments at the barbed end. Rho family GTPases activate Diaphanous-related formins through the relief of an autoregulatory interaction. The crystal structures of the N-terminal domains of human FMNL1 and FMNL2 in complex with active Cdc42 show that Cdc42 mediates contacts with all five armadillo repeats of the formin with specific interactions formed by the Rho-GTPase insert helix. Mutation of three residues within Rac1 results in a gain-of-function mutation for FMNL2 binding and reconstitution of the Cdc42 phenotype in vivo. Dimerization of FMNL1 through a parallel coiled coil segment leads to formation of an umbrella-shaped structure that—together with Cdc42—spans more than 15 nm in diameter. The two interacting FMNL-Cdc42 heterodimers expose six membrane interaction motifs on a convex protein surface, the assembly of which may facilitate actin filament elongation at the leading edge of lamellipodia and filopodia. PubMed: 25963737DOI: 10.1038/ncomms8088 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.8 Å) |
Structure validation
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