This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ksg

From Proteopedia

Revision as of 20:06, 2 May 2008 by OCA (Talk | contribs)
Jump to: navigation, search

Template:STRUCTURE 1ksg

Complex of Arl2 and PDE delta, Crystal Form 1


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

1KSG 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 23:06:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools