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CDC42/ACK GTPASE-BINDING DOMAIN COMPLEX

Overview

The proteins Cdc42 and Rac are members of the Rho family of small GTPases, (G proteins), which control signal-transduction pathways that lead to, rearrangements of the cell cytoskeleton, cell differentiation and cell, proliferation. They do so by binding to downstream effector proteins. Some, of these, known as CRIB (for Cdc42/Rac interactive-binding) proteins, bind, to both Cdc42 and Rac, such as the PAK1-3 serine/threonine kinases, whereas others are specific for Cdc42, such as the ACK tyrosine kinases, and the Wiscott-Aldrich-syndrome proteins (WASPs). The effector loop of, Cdc42 and Rac (comprising residues 30-40, also called switch I), is one of, two regions which change conformation on exchange of GDP for GTP. This, region is almost identical in Cdc42 and Racs, indicating that it does not, determine the specificity of these G proteins. Here we report the solution, structure of the complex of Cdc42 with the GTPase-binding domain ofACK., Both proteins undergo significant conformational changes on binding, to, form a new type of G-protein/effector complex. The interaction extends the, beta-sheet in Cdc42 by binding an extended strand from ACK, as seen in, Ras/effector interactions, but it also involves other regions of the G, protein that are important for determining the specificity of effector, binding.

About this Structure

1CF4 is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK., Mott HR, Owen D, Nietlispach D, Lowe PN, Manser E, Lim L, Laue ED, Nature. 1999 May 27;399(6734):384-8. PMID:10360579

Page seeded by OCA on Fri Feb 15 15:35:28 2008