1QAU
UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX
Summary for 1QAU
| Entry DOI | 10.2210/pdb1qau/pdb |
| Descriptor | NEURONAL NITRIC OXIDE SYNTHASE (RESIDUES 1-130) (2 entities in total) |
| Functional Keywords | beta-finger, oxidoreductase |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cell membrane, sarcolemma; Peripheral membrane protein (By similarity): P29476 |
| Total number of polymer chains | 1 |
| Total formula weight | 12032.88 |
| Authors | Hillier, B.J.,Christopherson, K.S.,Prehoda, K.E.,Bredt, D.S.,Lim, W.A. (deposition date: 1999-03-29, release date: 1999-05-04, Last modification date: 2024-02-14) |
| Primary citation | Hillier, B.J.,Christopherson, K.S.,Prehoda, K.E.,Bredt, D.S.,Lim, W.A. Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex. Science, 284:812-815, 1999 Cited by PubMed Abstract: The PDZ protein interaction domain of neuronal nitric oxide synthase (nNOS) can heterodimerize with the PDZ domains of postsynaptic density protein 95 and syntrophin through interactions that are not mediated by recognition of a typical carboxyl-terminal motif. The nNOS-syntrophin PDZ complex structure revealed that the domains interact in an unusual linear head-to-tail arrangement. The nNOS PDZ domain has two opposite interaction surfaces-one face has the canonical peptide binding groove, whereas the other has a beta-hairpin "finger." This nNOS beta finger docks in the syntrophin peptide binding groove, mimicking a peptide ligand, except that a sharp beta turn replaces the normally required carboxyl terminus. This structure explains how PDZ domains can participate in diverse interaction modes to assemble protein networks. PubMed: 10221915DOI: 10.1126/science.284.5415.812 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.25 Å) |
Structure validation
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