2j5x

From Proteopedia

Revision as of 17:40, 18 December 2007

STRUCTURE OF THE SMALL G PROTEIN ARF6 IN COMPLEX WITH GTPGAMMAS

Overview

The small GTP-binding protein Arf6 coordinates membrane traffic at the, plasma membrane with aspects of cytoskeleton organization. This function, does not overlap with that of other members of the ADP-ribosylation factor, (Arf) family, although their switch regions, which are their major sites, of interaction with regulators and effectors, have virtually identical, sequences. Here we report the crystal structure of full-length, non-myristoylated human Arf6 bound to GTPgammaS. Unlike their GDP-bound, forms, the active forms of Arf6 and Arf1 are very similar. Thus, the, switch regions are discriminatory elements between Arf isoforms in their, inactive but not in their active forms, a property that may generalize to, other families of small G proteins. This suggests that GTP-bound Arfs may, establish specific interactions outside the switch regions and/or be, recognized in their cellular context rather than as isolated proteins. The, structure also allows further insight into the lack of spontaneous GTPase, activity of Arf proteins.

About this Structure

2J5X is a Single protein structure of sequence from Homo sapiens with MG and GSP as ligands. This structure superseeds the now removed PDB entry 1HFV. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

The structural GDP/GTP cycle of human Arf6., Pasqualato S, Menetrey J, Franco M, Cherfils J, EMBO Rep. 2001 Mar;2(3):234-8. PMID:11266366

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