| First Author | Hanzal-Bayer M | Year | 2002 |
| Journal | EMBO J | Volume | 21 |
| Issue | 9 | Pages | 2095-106 |
| PubMed ID | 11980706 | Mgi Jnum | J:116350 |
| Mgi Id | MGI:3694136 | Doi | 10.1093/emboj/21.9.2095 |
| Citation | Hanzal-Bayer M, et al. (2002) The complex of Arl2-GTP and PDE delta: from structure to function. EMBO J 21(9):2095-106 |
| abstractText | 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 PDE delta 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. PDE delta is structurally closely related to RhoGDI and contains a deep empty hydrophobic pocket. Further experiments show that H-Ras, Rheb, Rho6 and G alpha(i1) interact with PDE delta and that, at least for H-Ras, the intact C-terminus is required. We suggest PDE delta to be a specific soluble transport factor for certain prenylated proteins and Arl2-GTP a regulator of PDE delta-mediated transport. |
