Solution structure of the extended neuronal nitric oxide synthase PDZ domain complexed with an associated peptide
The PDZ domain of neuronal nitric oxide synthase (nNOS) functions as a scaffold for
organizing the signal transduction complex of the enzyme. The NMR structure of a complex
composed of the nNOS PDZ domain and an associated peptide suggests that a two-
stranded β-sheet C-terminal to the canonical PDZ domain may mediate its interaction with
the PDZ domains of postsynaptic density-95 and α-syntrophin. The structure also provides
the molecular basis of recognition of Asp–X–Val–COOH peptides by the nNOS PDZ domain …
organizing the signal transduction complex of the enzyme. The NMR structure of a complex
composed of the nNOS PDZ domain and an associated peptide suggests that a two-
stranded β-sheet C-terminal to the canonical PDZ domain may mediate its interaction with
the PDZ domains of postsynaptic density-95 and α-syntrophin. The structure also provides
the molecular basis of recognition of Asp–X–Val–COOH peptides by the nNOS PDZ domain …
Abstract
The PDZ domain of neuronal nitric oxide synthase (nNOS) functions as a scaffold for organizing the signal transduction complex of the enzyme. The NMR structure of a complex composed of the nNOS PDZ domain and an associated peptide suggests that a two-stranded β-sheet C-terminal to the canonical PDZ domain may mediate its interaction with the PDZ domains of postsynaptic density-95 and α-syntrophin. The structure also provides the molecular basis of recognition of Asp–X–Val–COOH peptides by the nNOS PDZ domain. The role of the C-terminal extension in Asp-X-Val-COOH peptide binding is investigated. Additionally, NMR studies further show that the Asp-X-Val-COOH peptide and a C-terminal peptide from a novel cytosolic protein named CAPON bind to the same pocket of the nNOS PDZ domain.
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