2ogp

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Revision as of 09:26, 23 January 2008

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Solution structure of the second PDZ domain of Par-3

Overview

Multiple PDZ domain scaffold protein Par-3 and phosphoinositides (PIPs), are required for polarity in diverse cell types. We show that the second, PDZ domain of Par-3 binds to phosphatidylinositol (PI) lipid membranes, with high affinity. We further demonstrate that a large subset of PDZ, domains in mammalian genomes are capable of binding to PI lipid membranes, indicating that lipid binding is the second most prevalent interaction, mode of PDZ domains known to date. The biochemical and structural basis of, Par-3 PDZ2-mediated membrane interaction is characterized in detail. The, membrane binding capacity of Par-3 PDZ2 is critical for epithelial cell, polarization. Interestingly, the lipid phosphatase PTEN directly binds to, the third PDZ domain of Par-3. The concatenation of the PIP-binding PDZ2, and the lipid phosphatase PTEN-binding PDZ3 endows Par-3 as an ideal, scaffold protein for integrating PIP signaling events during cellular, polarization.

About this Structure

2OGP is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

PDZ domains of par-3 as potential phosphoinositide signaling integrators., Wu H, Feng W, Chen J, Chan LN, Huang S, Zhang M, Mol Cell. 2007 Dec 14;28(5):886-98. PMID:18082612

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