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2ogp
From Proteopedia
| 2ogp, 20 NMR models () | |||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Solution structure of the second PDZ domain of Par-3
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2OGP is a 1 chain structure of sequence from Rattus norvegicus. Full experimental information is available from OCA.
Reference
- Wu H, Feng W, Chen J, Chan LN, Huang S, Zhang M. PDZ domains of Par-3 as potential phosphoinositide signaling integrators. Mol Cell. 2007 Dec 14;28(5):886-98. PMID:18082612 doi:10.1016/j.molcel.2007.10.028
Page seeded by OCA on Tue Feb 17 13:39:21 2009
Categories: Rattus norvegicus | Chan, L N. | Chen, J. | Feng, W. | Wu, H. | Zhang, M. | Cell polarity | Par-3 | Pdz domain | Signaling protein
