4js9: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4js9|  PDB=4js9  |  SCENE=  }}
===Structural Characterization of Inducible Nitric Oxide Synthase Substituted With Mesoheme===


The entry 4js9 is ON HOLD until Paper Publication
==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>  


Authors: Hannibal, L., Page, R.C., Bolisetty, K., Yu, Z., Misra, S., Stuehr, D.J.
==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].  


Description: Structural Characterization of Inducible Nitric Oxide Synthase Substituted With Mesoheme
==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

Template:STRUCTURE 4js9

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

  1. ↑ 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:https://dx.doi.org/10.1126/science.1119407

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