5I7Z
Crystal structure of a Par-6 PDZ-Crumbs 3 C-terminal peptide complex
Summary for 5I7Z
| Entry DOI | 10.2210/pdb5i7z/pdb |
| Descriptor | LD29223p, Crb-3, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
| Functional Keywords | pdz, cell polarity, signaling protein |
| Biological source | Drosophila melanogaster (Fruit fly) More |
| Total number of polymer chains | 2 |
| Total formula weight | 11340.05 |
| Authors | Whitney, D.S.,Peterson, F.C.,Prehoda, K.E.,Volkman, B.F. (deposition date: 2016-02-18, release date: 2016-03-16, Last modification date: 2024-03-06) |
| Primary citation | Whitney, D.S.,Peterson, F.C.,Kittell, A.W.,Egner, J.M.,Prehoda, K.E.,Volkman, B.F. Binding of Crumbs to the Par-6 CRIB-PDZ Module Is Regulated by Cdc42. Biochemistry, 55:1455-1461, 2016 Cited by PubMed Abstract: Par-6 is a scaffold protein that organizes other proteins into a complex required to initiate and maintain cell polarity. Cdc42-GTP binds the CRIB module of Par-6 and alters the binding affinity of the adjoining PDZ domain. Allosteric regulation of the Par-6 PDZ domain was first demonstrated using a peptide identified in a screen of typical carboxyl-terminal ligands. Crumbs, a membrane protein that localizes a conserved polarity complex, was subsequently identified as a functional partner for Par-6 that likely interacts with the PDZ domain. Here we show by nuclear magnetic resonance that Par-6 binds a Crumbs carboxyl-terminal peptide and report the crystal structure of the PDZ-peptide complex. The Crumbs peptide binds Par-6 more tightly than the previously studied carboxyl peptide ligand and interacts with the CRIB-PDZ module in a Cdc42-dependent manner. The Crumbs:Par-6 crystal structure reveals specific PDZ-peptide contacts that contribute to its higher affinity and Cdc42-enhanced binding. Comparisons with existing structures suggest that multiple C-terminal Par-6 ligands respond to a common conformational switch that transmits the allosteric effects of GTPase binding. PubMed: 26894406DOI: 10.1021/acs.biochem.5b01342 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.801 Å) |
Structure validation
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