Structure of Cdc42 bound to the GTPase binding domain of PAK

Citation
A. Morreale et al., Structure of Cdc42 bound to the GTPase binding domain of PAK, NAT ST BIOL, 7(5), 2000, pp. 384-388
Citations number
31
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
NATURE STRUCTURAL BIOLOGY
ISSN journal
1072-8368 → ACNP
Volume
7
Issue
5
Year of publication
2000
Pages
384 - 388
Database
ISI
SICI code
1072-8368(200005)7:5<384:SOCBTT>2.0.ZU;2-C
Abstract
The Rho family GTPases, Cdc42, Rac and Rho, regulate signal transduction pa thways via interactions with downstream effector proteins. We report here t he solution structure of Cdc42 bound to the GTPase binding domain of alpha PAK, an effector of both Cdc42 and Rac The structure is compared with those of Cdc42 bound to similar fragments of ACR and WASP, two effector proteins that bind only to Cdc42. The N-termini of all three effector fragments bin d in an extended conformation to strand beta 2 of Cdc42, and contact helice s alpha 1 and alpha 5, The remaining residues bind to switches I and II of Cdc42, but in a significantly different manner. The structure, together wit h mutagenesis data suggests reasons for the specificity of these interactio ns and provides insight into the mechanism of PAK activation.