4js9
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | + | {{STRUCTURE_4js9| PDB=4js9 | SCENE= }} | |
+ | ===Structural Characterization of Inducible Nitric Oxide Synthase Substituted With Mesoheme=== | ||
- | + | ==Function== | |
+ | [[http://www.uniprot.org/uniprot/NOS2_MOUSE NOS2_MOUSE]] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.<ref>PMID:16373578</ref> | ||
- | + | ==About this Structure== | |
+ | [[4js9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JS9 OCA]. | ||
- | + | ==Reference== | |
+ | <references group="xtra"/><references/> | ||
+ | [[Category: Bolisetty, K.]] | ||
+ | [[Category: Hannibal, L.]] | ||
+ | [[Category: Misra, S.]] | ||
+ | [[Category: Page, R C.]] | ||
+ | [[Category: Stuehr, D J.]] | ||
+ | [[Category: Yu, Z.]] | ||
+ | [[Category: Calmodulin-binding]] | ||
+ | [[Category: Fad]] | ||
+ | [[Category: Fmn]] | ||
+ | [[Category: Iron]] | ||
+ | [[Category: Mesoheme]] | ||
+ | [[Category: Metal-binding]] | ||
+ | [[Category: Nadp]] | ||
+ | [[Category: Oxidoreductase]] |
Revision as of 07:53, 23 April 2014
Contents |
Structural Characterization of Inducible Nitric Oxide Synthase Substituted With Mesoheme
Function
[NOS2_MOUSE] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.[1]
About this Structure
4js9 is a 2 chain structure. Full crystallographic information is available from OCA.
Reference
- ↑ Kim SF, Huri DA, Snyder SH. Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2. Science. 2005 Dec 23;310(5756):1966-70. PMID:16373578 doi:http://dx.doi.org/10.1126/science.1119407
Categories: Bolisetty, K. | Hannibal, L. | Misra, S. | Page, R C. | Stuehr, D J. | Yu, Z. | Calmodulin-binding | Fad | Fmn | Iron | Mesoheme | Metal-binding | Nadp | Oxidoreductase