2LC7
Solution structure of the isolated Par-6 PDZ domain
Summary for 2LC7
| Entry DOI | 10.2210/pdb2lc7/pdb |
| Related | 2LC6 |
| NMR Information | BMRB: 17600 |
| Descriptor | Par-6 (1 entity in total) |
| Functional Keywords | crib, allostery, cell polarity, cell adhesion |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 10926.46 |
| Authors | Volkman, B.F.,Whitney, D.S.,Peterson, F.C. (deposition date: 2011-04-25, release date: 2011-11-30, Last modification date: 2024-05-15) |
| Primary citation | Whitney, D.S.,Peterson, F.C.,Volkman, B.F. A Conformational Switch in the CRIB-PDZ Module of Par-6. Structure, 19:1711-1722, 2011 Cited by PubMed Abstract: Here, we report a novel mechanism of PDZ (PSD-95/Dlg/ZO-1) domain regulation that distorts a conserved element of PDZ ligand recognition. The polarity regulator Par-6 assembles a conserved multiprotein complex and is directly modulated by the Rho GTPase Cdc42. Cdc42 binds the adjacent Cdc42/Rac interactive binding (CRIB) and PDZ domains of Par-6, increasing C-terminal ligand binding affinity by 10-fold. By solving structures of the isolated PDZ domain and a disulfide-stabilized CRIB-PDZ, we detected a conformational switch that controls affinity by altering the configuration of the conserved "GLGF" loop. As a result, lysine 165 is displaced from the PDZ core by an adjacent hydrophobic residue, disrupting coordination of the PDZ ligand-binding cleft. Stabilization of the CRIB:PDZ interface restores K165 to its canonical location in the binding pocket. We conclude that a unique "dipeptide switch" in the Par-6 PDZ transmits a signal for allosteric activation to the ligand-binding pocket. PubMed: 22078569DOI: 10.1016/j.str.2011.07.018 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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