1e0a

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

Revision as of 10:22, 21 February 2008


1e0a

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CDC42 COMPLEXED WITH THE GTPASE BINDING DOMAIN OF P21 ACTIVATED KINASE

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.

About 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.

Reference

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

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