1RY4
NMR Structure of the CRIB-PDZ module of Par-6
Summary for 1RY4
| Entry DOI | 10.2210/pdb1ry4/pdb |
| NMR Information | BMRB: 6126 |
| Descriptor | CG5884-PA (1 entity in total) |
| Functional Keywords | pdz, crib, cdc-42, cell polarization, polarity adaptor complex, cell adhesion |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 13759.75 |
| Authors | Peterson, F.C.,Penkert, R.R.,Volkman, B.F.,Prehoda, K.E. (deposition date: 2003-12-19, release date: 2004-03-23, Last modification date: 2024-05-22) |
| Primary citation | Peterson, F.C.,Penkert, R.R.,Volkman, B.F.,Prehoda, K.E. Cdc42 Regulates the Par-6 PDZ Domain through an Allosteric CRIB-PDZ Transition. Mol.Cell, 13:665-676, 2004 Cited by PubMed Abstract: 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. PubMed: 15023337DOI: 10.1016/S1097-2765(04)00086-3 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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