1QAV

Unexpected Modes of PDZ Domain Scaffolding Revealed by Structure of NNOS-Syntrophin Complex

Summary for 1QAV

• Entry DOI: 10.2210/pdb1qav/pdb
• Descriptor: ALPHA-1 SYNTROPHIN (RESIDUES 77-171), NEURONAL NITRIC OXIDE SYNTHASE (RESIDUES 1-130) (3 entities in total)
• Functional Keywords: beta-finger, heterodimer, membrane protein-oxidoreductase complex, membrane protein/oxidoreductase
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side: Q61234; Cell membrane, sarcolemma; Peripheral membrane protein (By similarity): P29476
• Total number of polymer chains: 2
• Total formula weight: 22012.47

Authors

Hillier, B.J.,Christopherson, K.S.,Prehoda, K.E.,Bredt, D.S.,Lim, W.A. (deposition date: 1999-03-30, 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

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: 10221915
DOI: 10.1126/science.284.5415.812

Experimental method

X-RAY DIFFRACTION (1.9 Å)