1Z2C
Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP
Summary for 1Z2C
| Entry DOI | 10.2210/pdb1z2c/pdb |
| Related | 1A2B 1UX5 1V9D 1Y64 |
| Descriptor | Rho-related GTP-binding protein RhoC, Diaphanous protein homolog 1, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | armadillo repeat, signaling protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cell membrane ; Lipid-anchor ; Cytoplasmic side : P08134 Cell membrane : O08808 |
| Total number of polymer chains | 4 |
| Total formula weight | 133561.27 |
| Authors | Rose, R.,Weyand, M.,Lammers, M.,Ishizaki, T.,Ahmadian, M.R.,Wittinghofer, A. (deposition date: 2005-03-08, release date: 2005-05-10, Last modification date: 2024-02-14) |
| Primary citation | Rose, R.,Weyand, M.,Lammers, M.,Ishizaki, T.,Ahmadian, M.R.,Wittinghofer, A. Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature, 435:513-518, 2005 Cited by PubMed Abstract: Formins are involved in a variety of cellular processes that require the remodelling of the cytoskeleton. They contain formin homology domains FH1 and FH2, which initiate actin assembly. The Diaphanous-related formins form a subgroup that is characterized by an amino-terminal Rho GTPase-binding domain (GBD) and an FH3 domain, which bind somehow to the carboxy-terminal Diaphanous autoregulatory domain (DAD) to keep the protein in an inactive conformation. Upon binding of activated Rho proteins, the DAD is released and the ability of the formin to nucleate and elongate unbranched actin filaments is induced. Here we present the crystal structure of RhoC in complex with the regulatory N terminus of mammalian Diaphanous 1 (mDia1) containing the GBD/FH3 region, an all-helical structure with armadillo repeats. Rho uses its 'switch' regions for interacting with two subdomains of GBD/FH3. We show that the FH3 domain of mDia1 forms a stable dimer and we also identify the DAD-binding site. Although binding of Rho and DAD on the N-terminal fragment of mDia1 are mutually exclusive, their binding sites are only partially overlapping. On the basis of our results, we propose a structural model for the regulation of mDia1 by Rho and DAD. PubMed: 15864301DOI: 10.1038/nature03604 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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