2JXO
Structure of the second PDZ domain of NHERF-1
Summary for 2JXO
| Entry DOI | 10.2210/pdb2jxo/pdb |
| NMR Information | BMRB: 15567 |
| Descriptor | Ezrin-radixin-moesin-binding phosphoprotein 50 (1 entity in total) |
| Functional Keywords | nherf-1, pdz domain, pdz2, acetylation, cell projection, membrane, phosphoprotein, polymorphism, wnt signaling pathway, protein binding |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm (By similarity): O14745 |
| Total number of polymer chains | 1 |
| Total formula weight | 10725.14 |
| Authors | |
| Primary citation | Cheng, H.,Li, J.,Fazlieva, R.,Dai, Z.,Bu, Z.,Roder, H. Autoinhibitory Interactions between the PDZ2 and C-terminal Domains in the Scaffolding Protein NHERF1 Structure, 17:660-669, 2009 Cited by PubMed Abstract: Na(+)/H(+) exchanger regulatory factor (NHERF1) is a signaling adaptor protein comprising two PDZ domains and a C-terminal ezrin-binding (EB) motif. To understand the role of intramolecular interactions in regulating its binding properties, we characterized the complex between the second PDZ domain PDZ2 and the C-terminal 242-358 fragment of NHERF1 using NMR and fluorescence methods. NMR chemical shift and relaxation data implicate 11 C-terminal residues in binding and, together with a thermodynamic analysis of mutant proteins, indicate that the EB region becomes helical when bound to PDZ2. Both specific contacts between PDZ2 and EB as well as nonspecific interactions involving a 100-residue flexible linker contribute to stabilizing two structurally distinct closed conformations of NHERF1. The affinity of mutant proteins for an extrinsic ligand is inversely related to the helix-forming propensity of the EB motif. The findings provide a structural framework for understanding how autoinhibitory interactions modulated the binding properties of NHERF1. PubMed: 19446522DOI: 10.1016/j.str.2009.03.009 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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