1B8Q

SOLUTION STRUCTURE OF THE EXTENDED NEURONAL NITRIC OXIDE SYNTHASE PDZ DOMAIN COMPLEXED WITH AN ASSOCIATED PEPTIDE

Summary for 1B8Q

• Entry DOI: 10.2210/pdb1b8q/pdb
• Descriptor: PROTEIN (NEURONAL NITRIC OXIDE SYNTHASE), PROTEIN (HEPTAPEPTIDE) (2 entities in total)
• Functional Keywords: pdz domain, nnos, nitric oxide synthase, oxidoreductase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cell membrane, sarcolemma; Peripheral membrane protein (By similarity): P29476
• Total number of polymer chains: 2
• Total formula weight: 14296.56

Authors

Tochio, H.,Zhang, Q.,Mandal, P.,Li, M.,Zhang, M. (deposition date: 1999-02-01, release date: 1999-04-29, Last modification date: 2023-12-27)

Primary citation

Tochio, H.,Zhang, Q.,Mandal, P.,Li, M.,Zhang, M.
Solution structure of the extended neuronal nitric oxide synthase PDZ domain complexed with an associated peptide.
Nat.Struct.Biol., 6:417-421, 1999

PubMed 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 beta-sheet C-terminal to the canonical PDZ domain may mediate its interaction with the PDZ domains of postsynaptic density-95 and alpha-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.

PubMed: 10331866
DOI: 10.1038/8216

Experimental method

SOLUTION NMR