Structural highlights
1fop is a 2 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , , , , |
| Related: | 4nse |
| Activity: | Nitric-oxide synthase (NADPH dependent), with EC number 1.14.13.39 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[NOS3_BOVIN] Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the endothelial nitric oxide synthase (NOS) heme domain complexed with NO reveals close hydrogen bonding interactions between NO and the terminal guanidino nitrogen of the substrate, L-arginine. Dioxygen is expected to bind in a similar mode which will facilitate proton abstraction from L-Arg to dioxygen, a required step for O-O bond cleavage. Structures of mechanism-based NOS inhibitors, N(5)-(1-iminoethyl)-L-ornithine and N-(3-(aminomethyl)benzyl)acetamidine, provide clues on how this class of compounds operate as suicide substrate inhibitors leading to heme oxidation.
Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors.,Li H, Raman CS, Martasek P, Masters BS, Poulos TL Biochemistry. 2001 May 8;40(18):5399-406. PMID:11331003[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li H, Raman CS, Martasek P, Masters BS, Poulos TL. Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors. Biochemistry. 2001 May 8;40(18):5399-406. PMID:11331003
