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Nitric oxide synthase 1 (neuronal)
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| PDB rendering based on 1b8q. |
| Available structures: 1b8q, 1f20, 1k2r, 1k2s, 1k2t, 1k2u, 1lzx, 1lzz, 1m00, 1mmv, 1mmw, 1om4, 1om5, 1p6h, 1p6i, 1p6j, 1p6k, 1qau, 1qav, 1qw6, 1qwc, 1rs6, 1rs7, 1tll, 1vag, 1zvi, 1zvl, 1zzq, 1zzr, 1zzu, 2g6h, 2g6i, 2g6j, 2g6k, 2g6l, 2g6m, 2g6n, 2hx3, 2hx4 |
| Identifiers |
| Symbols |
NOS1; IHPS1; NOS |
| External IDs |
OMIM: 163731 MGI: 97360 HomoloGene: 37327 |
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| RNA expression pattern |
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More reference expression data
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| Orthologs |
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Human |
Mouse |
| Entrez |
4842 |
18125 |
| Ensembl |
ENSG00000089250 |
ENSMUSG00000029361 |
| Uniprot |
P29475 |
Q9JJ30 |
| Refseq |
NM_000620 (mRNA)
NP_000611 (protein) |
XM_992536 (mRNA)
XP_997630 (protein) |
| Location |
Chr 12: 116.14 - 116.28 Mb |
Chr 5: 118.1 - 118.22 Mb |
| Pubmed search |
[1] |
[2] |
Nitric oxide synthase 1 (neuronal), also known as NOS1, is an enzyme which in humans is encoded by the NOS1 gene.[1][2]
Function
Nitric oxide (NO) is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter; it is implicated in neurotoxicity associated with stroke and neurodegenerative diseases, neural regulation of smooth muscle, including peristalsis, and penile erection. NO is also responsible for endothelium-derived relaxing factor activity regulating blood pressure. In macrophages, NO mediates tumoricidal and bactericidal actions, as indicated by the fact that inhibitors of NO synthase (NOS) block these effects. Neuronal NOS and macrophage NOS are distinct isoforms.[3] Both the neuronal and the macrophage forms are unusual among oxidative enzymes in requiring several electron donors: FAD, flavin mononucleotide (FMN), NADPH, and tetrahydrobiopterin.[4]
Clinical significance
It has been implicated in asthma,[5][6] schizophrenia[7][8] and restless leg syndrome.[9] It has also been investigated with respect to bipolar disorder.[10]
Interactions
NOS1 has been shown to interact with DLG4[11][12] and NOS1AP.[11]
See also
References
- ^ Kishimoto J, Spurr N, Liao M, Lizhi L, Emson P, Xu W (November 1992). "Localization of brain nitric oxide synthase (NOS) to human chromosome 12". Genomics 14 (3): 802–4. doi:10.1016/S0888-7543(05)80192-2. PMID 1385308.
- ^ Geller DA, Lowenstein CJ, Shapiro RA, Nussler AK, Di Silvio M, Wang SC, Nakayama DK, Simmons RL, Snyder SH, Billiar TR (April 1993). "Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes". Proc. Natl. Acad. Sci. U.S.A. 90 (8): 3491–5. doi:10.1073/pnas.90.8.3491. PMID 7682706.
- ^ Lowenstein CJ, Glatt CS, Bredt DS, Snyder SH (August 1992). "Cloned and expressed macrophage nitric oxide synthase contrasts with the brain enzyme". Proc. Natl. Acad. Sci. U.S.A. 89 (15): 6711–5. doi:10.1073/pnas.89.15.6711. PMID 1379716.
- ^ "Entrez Gene: NOS1 Nitric oxide synthase 1 (neuronal)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4843.
- ^ Grasemann H, Yandava CN, Drazen JM (December 1999). "Neuronal NO synthase (NOS1) is a major candidate gene for asthma". Clin. Exp. Allergy 29 Suppl 4: 39–41. PMID 10641565. http://www3.interscience.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0954-7894&date=1999&volume=29&issue=&spage=39.
- ^ Leung TF, Liu EK, Tang NL, Ko FW, Li CY, Lam CW, Wong GW (October 2005). "Nitric oxide synthase polymorphisms and asthma phenotypes in Chinese children". Clin. Exp. Allergy 35 (10): 1288–94. doi:10.1111/j.1365-2222.2005.02342.x. PMID 16238787.
- ^ Shinkai T, Ohmori O, Hori H, Nakamura J (2002). "Allelic association of the neuronal nitric oxide synthase (NOS1) gene with schizophrenia". Mol. Psychiatry 7 (6): 560–3. doi:10.1038/sj.mp.4001041. PMID 12140778.
- ^ Reif A, Herterich S, Strobel A, Ehlis AC, Saur D, Jacob CP, Wienker T, Töpner T, Fritzen S, Walter U, Schmitt A, Fallgatter AJ, Lesch KP (March 2006). "A neuronal nitric oxide synthase (NOS-I) haplotype associated with schizophrenia modifies prefrontal cortex function". Mol. Psychiatry 11 (3): 286–300. doi:10.1038/sj.mp.4001779. PMID 16389274.
- ^ Winkelmann J, Lichtner P, Schormair B, Uhr M, Hauk S, Stiasny-Kolster K, Trenkwalder C, Paulus W, Peglau I, Eisensehr I, Illig T, Wichmann HE, Pfister H, Golic J, Bettecken T, Pütz B, Holsboer F, Meitinger T, Müller-Myhsok B (February 2008). "Variants in the neuronal nitric oxide synthase (nNOS, NOS1) gene are associated with restless legs syndrome". Mov. Disord. 23 (3): 350–8. doi:10.1002/mds.21647. PMID 18058820.
- ^ Buttenschön HN, Mors O, Ewald H, McQuillin A, Kalsi G, Lawrence J, Gurling H, Kruse TA (January 2004). "No association between a neuronal nitric oxide synthase (NOS1) gene polymorphism on chromosome 12q24 and bipolar disorder". Am. J. Med. Genet. B Neuropsychiatr. Genet. 124B (1): 73–5. doi:10.1002/ajmg.b.20040. PMID 14681919.
- ^ a b Jaffrey, S R; Snowman A M, Eliasson M J, Cohen N A, Snyder S H (Jan. 1998). "CAPON: a protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95". Neuron (UNITED STATES) 20 (1): 115-24. ISSN 0896-6273. PMID 9459447.
- ^ Brenman, J E; Chao D S, Gee S H, McGee A W, Craven S E, Santillano D R, Wu Z, Huang F, Xia H, Peters M F, Froehner S C, Bredt D S (Mar. 1996). "Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains". Cell (UNITED STATES) 84 (5): 757-67. ISSN 0092-8674. PMID 8625413.
Further reading
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PDB Gallery |
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1b8q: SOLUTION STRUCTURE OF THE EXTENDED NEURONAL NITRIC OXIDE SYNTHASE PDZ DOMAIN COMPLEXED WITH AN ASSOCIATED PEPTIDE
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1f20: CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE FAD/NADP+ DOMAIN AT 1.9A RESOLUTION.
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1k2r: Structure of rat brain nNOS heme domain complexed with NG-nitro-L-arginine
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1k2s: Structure of rat brain nNOS heme domain complexed with NG-allyl-L-arginine
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1k2t: Structure of rat brain nNOS heme domain complexed with S-ethyl-N-phenyl-isothiourea
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1k2u: Structure of rat brain nNOS heme domain complexed with S-ethyl-N-[4-(trifluoromethyl)phenyl] isothiourea
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1lzx: Rat neuronal NOS heme domain with NG-hydroxy-L-arginine bound
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1lzz: Rat neuronal NOS heme domain with N-isopropyl-N'-hydroxyguanidine bound
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1m00: Rat neuronal NOS heme domain with N-butyl-N'-hydroxyguanidine bound
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1mmv: Rat neuronal NOS heme domain with NG-propyl-L-arginine bound
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1mmw: Rat neuronal NOS heme domain with vinyl-L-NIO bound
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1om4: STRUCTURE OF RAT NEURONAL NOS HEME DOMAIN WITH L-ARGININE BOUND
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1om5: STRUCTURE OF RAT NEURONAL NOS HEME DOMAIN WITH 3-BROMO-7-NITROINDAZOLE BOUND
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1p6h: Rat neuronal NOS heme domain with L-N(omega)-nitroarginine-2,4-L-diaminobutyric amide bound
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1p6i: Rat neuronal NOS heme domain with (4S)-N-(4-amino-5-[aminoethyl]aminopentyl)-N'-nitroguanidine bound
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1p6j: Rat neuronal NOS heme domain with L-N(omega)-nitroarginine-(4R)-amino-L-proline amide bound
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1p6k: Rat neuronal NOS D597N mutant heme domain with L-N(omega)-nitroarginine-2,4-L-diaminobutyric amide bound
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1qau: UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX
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1qav: Unexpected Modes of PDZ Domain Scaffolding Revealed by Structure of NNOS-Syntrophin Complex
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1qw6: Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.
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1qwc: Rat neuronal nitric oxide synthase oxygenase domain in complex with W1400 inhibitor.
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1rs6: Rat neuronal NOS heme domain with D-lysine-D-nitroarginine amide bound
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1rs7: Rat neuronal NOS heme domain with D-phenylalanine-D-nitroarginine amide bound
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1tll: CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE REDUCTASE MODULE AT 2.3 A RESOLUTION.
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1vag: Neuronal nitric oxide synthase oxygenase domain complexed with the inhibitor AR-R17477
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1zvi: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain
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1zvl: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain complexed with natural substrate L-Arg.
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1zzq: Rat nNOS D597N mutant with L-N(omega)-Nitroarginine-(4R)-amino-L-proline amide bound
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1zzr: Rat nNOS D597N/M336V double mutant with L-N(omega)-Nitroarginine-(4R)-amino-L-proline amide bound
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1zzu: Rat nNOS D597N/M336V double mutant with L-N(omega)-Nitroarginine-2,4-L-Diaminobutyric Amide Bound
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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