1QWC

Rat neuronal nitric oxide synthase oxygenase domain in complex with W1400 inhibitor.

1QWC の概要

• エントリーDOI: 10.2210/pdb1qwc/pdb
• 関連するPDBエントリー: 1QW4 1QW5 1QW6
• 分子名称: Nitric-oxide synthase, brain, ZINC ION, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• 機能のキーワード: rat nnosoxy w1400 inhibitor complex, oxidoreductase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cell membrane, sarcolemma ; Peripheral membrane protein : P29476
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49680.59

構造登録者

Fedorov, R.,Hartmann, E.,Ghosh, D.K.,Schlichting, I. (登録日: 2003-09-02, 公開日: 2003-12-09, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)