1ksh
From Proteopedia
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'''Complex of Arl2 and PDE delta, Crystal Form 2 (native)''' | '''Complex of Arl2 and PDE delta, Crystal Form 2 (native)''' | ||
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[[Category: Roversi, P.]] | [[Category: Roversi, P.]] | ||
[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
| - | [[Category: | + | [[Category: Arf family]] |
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| - | [[Category: | + | [[Category: Immunoglobuline-like fold]] |
| - | [[Category: | + | [[Category: Small gtp-binding protein]] |
| - | [[Category: | + | [[Category: Small gtpase]] |
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Revision as of 20:06, 2 May 2008
Complex of Arl2 and PDE delta, Crystal Form 2 (native)
Overview
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.
About this Structure
1KSH is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
The complex of Arl2-GTP and PDE delta: from structure to function., Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC, EMBO J. 2002 May 1;21(9):2095-106. PMID:11980706 Page seeded by OCA on Fri May 2 23:06:55 2008
