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Nos1

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Revision as of 18:35, 12 April 2016

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You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

1 Location
2 Function
3 Disease
4 Relevance
5 Structural highlights

Location

The human gene NOS1, found on chromosome 12, encodes for a nitric oxide synthase. Nitric oxide synthases consume L-arginine to produce nitric oxide. The chemical equation is shown below.

2 L-arginine + 3 NADPH + 4 O(2) = 2 L- citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O

Nitric oxide is used in a wide variety of processes. A few examples of molecular processes include heme binding, NADP binding, calcium signaling, and oxidation-reduction reactions. Biological examples include regulation of cardiac muscle contraction, blood coagulation, aging, and regulation of neurogenesis. There are three known isoforms known for NOS1 in humans produced by alternative splicing. These isoforms are reffered to as neuronal NOS (nNOS), endothelial NOS (eNOS), and cytokine-inducible NOS (iNOS).

Function

Disease

Relevance

Structural highlights

Nos exists as a homodimer. This homodimer consists of two regions. One region is an N-terminal oxygenase domain and the other is a C-terminal reductase. The N-terminal oxygenase domain is an extended beta sheet cage with binding sites for heme and pterin. Nos has a N-terminal catalytic domain with a heme active site. Nos 1 also has a cofactor site nearby for tetrahydrobiopterin (H4B). Nos has a C-terminal reductase domain containing FMN, FAD and NADPH binding sites. Electrons are passed from FAD to FMN and then to the heme. This electron flow is controlled by the binding of CaM and Ca2+ in the linker region between the two major domains. The linker between the oxygenase and reductase domains contains a calmodulin-binding sequence. Nos1 is found in neuronal tissue.

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References

↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Proteopedia Page Contributors and Editors (what is this?)

Mark T. Hilliard, Michal Harel

Retrieved from "http://52.214.119.220/wiki/index.php/Nos1"

@@ Line 9: / Line 9: @@
 L-arginine + 3 NADPH + 4 O(2) = 2 L- citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O
-Nitric oxide is used in a wide variety of processes. A few examples of molecular processes include heme binding, NADP binding, calcium signaling, and oxidation-reduction reactions. Biological examples include regulation of cardiac muscle contraction, blood coagulation, aging, and regulation of neurogenesis. There are five known isoforms known for NOS1 in humans produced by alternative splicing, which are expressed at different levels as denoted by microarray data. Please note that microarray data is only available for isoforms 1, 3, and 4.
+Nitric oxide is used in a wide variety of processes. A few examples of molecular processes include heme binding, NADP binding, calcium signaling, and oxidation-reduction reactions. Biological examples include regulation of cardiac muscle contraction, blood coagulation, aging, and regulation of neurogenesis. There are three known isoforms known for NOS1 in humans produced by alternative splicing. These isoforms are reffered to as neuronal NOS (nNOS), endothelial NOS (eNOS), and cytokine-inducible NOS (iNOS).
-Tissue	        Isoform 1	Isoform 3	Isoform 4
-Skeletal muscle	Moderate	N/A	        Moderate
-Brain           Moderate	N/A	        Low
-Testis	        Moderate	Moderate	Moderate
-Lung	        Moderate	N/A	        Moderate
-Kidney	        Moderate	N/A	        Moderate
-Heart	        Low	        N/A	        N/A
-Adrenal gland	Low	        N/A	        N/A
-Retina	        Low	        N/A	        N/A
-[[Image:expression table snip.jpg]]
 == Function ==

Nos1

From Proteopedia

Revision as of 18:35, 12 April 2016

Your Heading Here (maybe something like 'Structure')

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