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- Title
The complex of Arl2-GTP and PDEd: from structure to function.
- Authors
Hanzal-Bayer, Michael; Renault, Louis; Roversi, Pietro; Wittinghofer, Alfred; Hillig, Roman C.
- Abstract
Arf-like (Arl) proteins are close relatives of the Arf regulators of vesicular transport, but their function is unknown. Here, we present the crystal structure of full-length Arl2-GTP in complex with its effector PDEδ solved in two crystal forms (Protein Data Bank codes 1KSG, 1KSH and 1KSJ). Arl2 shows a dramatic conformational change from the GDP-bound form, which suggests that it is reversibly membrane associated. PDEδ is structurally closely related to RhoGDI and contains a deep empty hydrophobic pocket. Further experiments show that H-Ras, Rheb, Rho6 and Gαil interact with PDEδ and that, at least for H-Ras, the intact C-terminus is required. We suggest PDEδ to be a specific soluble transport factor for certain prenylated proteins and Arl2-GTP a regulator of PDEδ-mediated transport.
- Subjects
PROTEINS; CRYSTALS; VESICULAR stomatitis; STOMATITIS in animals; BIOMOLECULES; ORGANIC compounds
- Publication
EMBO Journal, 2002, Vol 21, Issue 9, p2095
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1093/emboj/21.9.2095