1zsg: Difference between revisions

Revision as of 19:12, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1zsg.png

Template:STRUCTURE 1zsg

beta PIX-SH3 complexed with an atypical peptide from alpha-PAKbeta PIX-SH3 complexed with an atypical peptide from alpha-PAK

Template:ABSTRACT PUBMED 16101281

About this StructureAbout this Structure

1ZSG is a Protein complex structure of sequences from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Structural analysis of the SH3 domain of beta-PIX and its interaction with alpha-p21 activated kinase (PAK)., Mott HR, Nietlispach D, Evetts KA, Owen D, Biochemistry. 2005 Aug 23;44(33):10977-83. PMID:16101281

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OCA

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-'''beta PIX-SH3 complexed with an atypical peptide from alpha-PAK'''
+===beta PIX-SH3 complexed with an atypical peptide from alpha-PAK===
-==Overview==
+<!--
-The PAK Ser/Thr kinases are important downstream effectors of the Rho family GTPases Cdc42 and Rac, partly mediating the role of these G proteins in cell proliferation and cytoskeletal rearrangements. As well as small G proteins, PAK interacts with the Cdc42/Rac exchange factor beta-PIX via the PIX SH3 domain and a nontypical Pro-rich region in PAK. This interaction is thought to affect the localization of PAK, as well as increased GTP/GDP exchange of Rac and Cdc42. We have determined the structure of the PIX-SH3/PAK peptide complex and shown that it differs from typical Src-like SH3/peptide complexes. The peptide makes contacts through the Pro-rich sequence in a similar way to standard SH3/peptide complexes, even though the Pro residue positions are not conserved. In addition, there are interactions with a Pro and Lys in the PAK, which are C-terminal to the conserved Arg found in all SH3-binding sequences. These contact a fourth binding pocket on the SH3 domain. We have measured the affinity of PIX-SH3 for the PAK peptide and found that it is of intermediate affinity. When PAK is activated, Ser-199 in the PIX-binding site is phosphorylated. This phosphorylation is sufficient to reduce the affinity for PIX 6-fold.
+The line below this paragraph, {{ABSTRACT_PUBMED_16101281}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16101281 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16101281}}
 ==About this Structure==
-ZSG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZSG OCA].
+ZSG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZSG OCA].
 ==Reference==
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 [[Category: Owen, D.]]
 [[Category: Sh3-peptide complex]]
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