1ry4: Difference between revisions
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{{STRUCTURE_1ry4| PDB=1ry4 | SCENE= }} | |||
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'''NMR Structure of the CRIB-PDZ module of Par-6''' | '''NMR Structure of the CRIB-PDZ module of Par-6''' | ||
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[[Category: Prehoda, K E.]] | [[Category: Prehoda, K E.]] | ||
[[Category: Volkman, B F.]] | [[Category: Volkman, B F.]] | ||
[[Category: | [[Category: Cdc-42]] | ||
[[Category: | [[Category: Cell polarization]] | ||
[[Category: | [[Category: Crib]] | ||
[[Category: | [[Category: Pdz]] | ||
[[Category: | [[Category: Polarity adaptor complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:03:03 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 08:03, 3 May 2008
NMR Structure of the CRIB-PDZ module of Par-6
OverviewOverview
Regulation of protein interaction domains is required for cellular signaling dynamics. Here, we show that the PDZ protein interaction domain from the cell polarity protein Par-6 is regulated by the Rho GTPase Cdc42. Cdc42 binds to a CRIB domain adjacent to the PDZ domain, increasing the affinity of the Par-6 PDZ for its carboxy-terminal ligand by approximately 13-fold. Par-6 PDZ regulation is required for function as mutational disruption of Cdc42-Par-6 PDZ coupling leads to inactivation of Par-6 in polarized MDCK epithelial cells. Structural analysis reveals that the free PDZ domain has several deviations from the canonical PDZ conformation that account for its low ligand affinity. Regulation results from a Cdc42-induced conformational transition in the CRIB-PDZ module that causes the PDZ to assume a canonical, high-affinity PDZ conformation. The coupled CRIB and PDZ architecture of Par-6 reveals how simple binding domains can be combined to yield complex regulation.
About this StructureAbout this Structure
1RY4 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition., Peterson FC, Penkert RR, Volkman BF, Prehoda KE, Mol Cell. 2004 Mar 12;13(5):665-76. PMID:15023337 Page seeded by OCA on Sat May 3 08:03:03 2008