1QW6

Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.

Summary for 1QW6

• Entry DOI: 10.2210/pdb1qw6/pdb
• Related: 1QW4 1QW5
• Descriptor: Nitric-oxide synthase, brain, ZINC ION, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• Functional Keywords: rat nnosoxy complex with n-omega-propyl-l-arg, oxidoreductase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cell membrane, sarcolemma ; Peripheral membrane protein : P29476
• Total number of polymer chains: 1
• Total formula weight: 49720.64

Authors

Fedorov, R.,Hartmann, E.,Ghosh, D.K.,Schlichting, I. (deposition date: 2003-09-01, release date: 2003-12-09, Last modification date: 2024-02-14)

Primary citation

Fedorov, R.,Hartmann, E.,Ghosh, D.K.,Schlichting, I.
Structural basis for the specificity of the nitric-oxide synthase inhibitors W1400 and Nomega-propyl-L-Arg for the inducible and neuronal isoforms.
J.Biol.Chem., 278:45818-45825, 2003

PubMed Abstract: The high level of amino acid conservation and structural similarity in the immediate vicinity of the substrate binding sites of the oxygenase domains of the nitric-oxide synthase (NOS) isoforms (eNOSoxy, iNOSoxy, and nNOSoxy) make the interpretation of the structural basis of inhibitor isoform specificity a challenge and provide few clues for the design of new selective compounds. Crystal structures of iNOSoxy and nNOSoxy complexed with the inhibitors W1400 and Nomega-propyl-l-arginine provide a rationale for their isoform specificity. It involves differences outside the immediate active site as well as a conformational flexibility in the active site that allows the adoption of distinct conformations in response to interactions with the inhibitors. This flexibility is determined by isoform-specific residues outside the active site.

PubMed: 12954642
DOI: 10.1074/jbc.M306030200

Experimental method

X-RAY DIFFRACTION (2.1 Å)