3NOS

HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE WITH ARGININE SUBSTRATE

3NOS の概要

• エントリーDOI: 10.2210/pdb3nos/pdb
• 関連するPDBエントリー: 4NOS
• 分子名称: ENDOTHELIAL NITRIC-OXIDE SYNTHASE, ZINC ION, N-OMEGA-HYDROXY-L-ARGININE, ... (6 entities in total)
• 機能のキーワード: l-arginine monooxygenase, nitric oxide, human, zns4, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane: P29474
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 98200.07

構造登録者

Fischmann, T.O.,Weber, P.C. (登録日: 1999-02-03, 公開日: 2000-02-04, 最終更新日: 2023-12-27)

主引用文献

Fischmann, T.O.,Hruza, A.,Niu, X.D.,Fossetta, J.D.,Lunn, C.A.,Dolphin, E.,Prongay, A.J.,Reichert, P.,Lundell, D.J.,Narula, S.K.,Weber, P.C.
Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation.
Nat.Struct.Biol., 6:233-242, 1999

PubMed Abstract: Crystal structures of human endothelial nitric oxide synthase (eNOS) and human inducible NOS (iNOS) catalytic domains were solved in complex with the arginine substrate and an inhibitor S-ethylisothiourea (SEITU), respectively. The small molecules bind in a narrow cleft within the larger active-site cavity containing heme and tetrahydrobiopterin. Both are hydrogen-bonded to a conserved glutamate (eNOS E361, iNOS E377). The active-site residues of iNOS and eNOS are nearly identical. Nevertheless, structural comparisons provide a basis for design of isozyme-selective inhibitors. The high-resolution, refined structures of eNOS (2.4 A resolution) and iNOS (2.25 A resolution) reveal an unexpected structural zinc situated at the intermolecular interface and coordinated by four cysteines, two from each monomer.

PubMed: 10074942
DOI: 10.1038/6675

実験手法

X-RAY DIFFRACTION (2.4 Å)