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[[Image:2nos.jpg|left|200px]]


{{Structure
==MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114), AMINOGUANIDINE COMPLEX==
|PDB= 2nos |SIZE=350|CAPTION= <scene name='initialview01'>2nos</scene>, resolution 2.3&Aring;
<StructureSection load='2nos' size='340' side='right'caption='[[2nos]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=AGU:AMINOGUANIDINE'>AGU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>
<table><tr><td colspan='2'>[[2nos]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NOS FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGU:AMINOGUANIDINE'>AGU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nos OCA], [https://pdbe.org/2nos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nos RCSB], [https://www.ebi.ac.uk/pdbsum/2nos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nos ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nos OCA], [http://www.ebi.ac.uk/pdbsum/2nos PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nos RCSB]</span>
== Function ==
}}
[https://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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/no/2nos_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2nos ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The nitric oxide synthase oxygenase domain (NOSox) oxidizes arginine to synthesize the cellular signal and defensive cytotoxin nitric oxide (NO). Crystal structures determined for cytokine-inducible NOSox reveal an unusual fold and heme environment for stabilization of activated oxygen intermediates key for catalysis. A winged beta sheet engenders a curved alpha-beta domain resembling a baseball catcher's mitt with heme clasped in the palm. The location of exposed hydrophobic residues and the results of mutational analysis place the dimer interface adjacent to the heme-binding pocket. Juxtaposed hydrophobic O2- and polar L-arginine-binding sites occupied by imidazole and aminoguanidine, respectively, provide a template for designing dual-function inhibitors and imply substrate-assisted catalysis.


'''MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114), AMINOGUANIDINE COMPLEX'''
The structure of nitric oxide synthase oxygenase domain and inhibitor complexes.,Crane BR, Arvai AS, Gachhui R, Wu C, Ghosh DK, Getzoff ED, Stuehr DJ, Tainer JA Science. 1997 Oct 17;278(5337):425-31. PMID:9334294<ref>PMID:9334294</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2nos" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The nitric oxide synthase oxygenase domain (NOSox) oxidizes arginine to synthesize the cellular signal and defensive cytotoxin nitric oxide (NO). Crystal structures determined for cytokine-inducible NOSox reveal an unusual fold and heme environment for stabilization of activated oxygen intermediates key for catalysis. A winged beta sheet engenders a curved alpha-beta domain resembling a baseball catcher's mitt with heme clasped in the palm. The location of exposed hydrophobic residues and the results of mutational analysis place the dimer interface adjacent to the heme-binding pocket. Juxtaposed hydrophobic O2- and polar L-arginine-binding sites occupied by imidazole and aminoguanidine, respectively, provide a template for designing dual-function inhibitors and imply substrate-assisted catalysis.
*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
 
== References ==
==About this Structure==
<references/>
2NOS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOS OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
The structure of nitric oxide synthase oxygenase domain and inhibitor complexes., Crane BR, Arvai AS, Gachhui R, Wu C, Ghosh DK, Getzoff ED, Stuehr DJ, Tainer JA, Science. 1997 Oct 17;278(5337):425-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9334294 9334294]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Nitric-oxide synthase]]
[[Category: Arvai AS]]
[[Category: Single protein]]
[[Category: Crane BR]]
[[Category: Arvai, A S.]]
[[Category: Getzoff ED]]
[[Category: Crane, B R.]]
[[Category: Stuehr DJ]]
[[Category: Getzoff, E D.]]
[[Category: Tainer JA]]
[[Category: Stuehr, D J.]]
[[Category: Tainer, J A.]]
[[Category: aminoguanidine]]
[[Category: heme]]
[[Category: l-arginine monooxygenase]]
[[Category: nitric oxide]]
[[Category: no]]
[[Category: no]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:06:07 2008''

Latest revision as of 08:21, 13 August 2026

MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114), AMINOGUANIDINE COMPLEX

2nos, resolution 2.30Å

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