Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex

Autor:	B J, Hillier, K S, Christopherson, K E, Prehoda, D S, Bredt, W A, Lim
Rok vydání:	1999
Předmět:	Protein Folding Binding Sites Protein Conformation Molecular Sequence Data Membrane Proteins Muscle Proteins Nitric Oxide Synthase Type I Crystallography X-Ray Ligands Protein Structure Secondary Dystrophin-Associated Proteins Amino Acid Sequence Nitric Oxide Synthase Dimerization Signal Transduction
Zdroj:	Science (New York, N.Y.). 284(5415)
ISSN:	0036-8075
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::c44796e01b3837cda6caae06f20cd33c https://pubmed.ncbi.nlm.nih.gov/10221915 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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