1e0a: Difference between revisions

Revision as of 13:22, 21 February 2008

CDC42 COMPLEXED WITH THE GTPASE BINDING DOMAIN OF P21 ACTIVATED KINASE

OverviewOverview

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.

About this StructureAbout this Structure

1E0A is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structure of Cdc42 bound to the GTPase binding domain of PAK., Morreale A, Venkatesan M, Mott HR, Owen D, Nietlispach D, Lowe PN, Laue ED, Nat Struct Biol. 2000 May;7(5):384-8. PMID:10802735

Page seeded by OCA on Thu Feb 21 12:22:25 2008

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OCA

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: Protein complex]]
 [[Category: Rattus norvegicus]]
-[[Category: Laue, E.D.]]
+[[Category: Laue, E D.]]
-[[Category: Lowe, P.N.]]
+[[Category: Lowe, P N.]]
 [[Category: Morreale, A.]]
-[[Category: Mott, H.R.]]
+[[Category: Mott, H R.]]
 [[Category: Nietlispach, D.]]
 [[Category: Owen, D.]]
@@ Line 25: / Line 25: @@
 [[Category: g protein signalling ser/thr kinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:41:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:25 2008''