1Z2C

Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP

1Z2C の概要

• エントリーDOI: 10.2210/pdb1z2c/pdb
• 関連するPDBエントリー: 1A2B 1UX5 1V9D 1Y64
• 分子名称: Rho-related GTP-binding protein RhoC, Diaphanous protein homolog 1, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: armadillo repeat, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane ; Lipid-anchor ; Cytoplasmic side : P08134; Cell membrane : O08808
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 133561.27

構造登録者

Rose, R.,Weyand, M.,Lammers, M.,Ishizaki, T.,Ahmadian, M.R.,Wittinghofer, A. (登録日: 2005-03-08, 公開日: 2005-05-10, 最終更新日: 2024-02-14)

主引用文献

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

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: 15864301
DOI: 10.1038/nature03604

実験手法

X-RAY DIFFRACTION (3 Å)