1E0A

Cdc42 complexed with the GTPase binding domain of p21 activated kinase

Summary for 1E0A

• Entry DOI: 10.2210/pdb1e0a/pdb
• Descriptor: Cell division control protein 42 homolog, Serine/threonine-protein kinase PAK 1, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total)
• Functional Keywords: signalling protein, g protein signalling ser/thr kinase, signalling protein-kinase complex, signalling protein/kinase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 26081.67

Authors

Morreale, A.,Venkatesan, M.,Mott, H.R.,Owen, D.,Nietlispach, D.,Lowe, P.N.,Laue, E.D. (deposition date: 2000-03-16, release date: 2000-04-18, Last modification date: 2024-05-15)

Primary citation

Morreale, A.,Venkatesan, M.,Mott, H.R.,Owen, D.,Nietlispach, D.,Lowe, P.N.,Laue, E.D.
Solution Structure of Cdc42 Bound to the Gtpase Binding Domian of Pak
Nat.Struct.Biol., 7:384-, 2000

PubMed Abstract: The Rho family GTPases, Cdc42, Rac and Rho, regulate signal transduction pathways via interactions with downstream effector proteins. We report here the solution structure of Cdc42 bound to the GTPase binding domain of alphaPAK, an effector of both Cdc42 and Rac. The structure is compared with those of Cdc42 bound to similar fragments of ACK and WASP, two effector proteins that bind only to Cdc42. The N-termini of all three effector fragments bind in an extended conformation to strand beta2 of Cdc42, and contact helices alpha1 and alpha5. The remaining residues bind to switches I and II of Cdc42, but in a significantly different manner. The structure, together with mutagenesis data, suggests reasons for the specificity of these interactions and provides insight into the mechanism of PAK activation.

PubMed: 10802735
DOI: 10.1038/75158

Experimental method

SOLUTION NMR