1nos: Difference between revisions

New page: left|200px<br /><applet load="1nos" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nos, resolution 2.1Å" /> '''MURINE INDUCIBLE NITR...
 
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[[Image:1nos.jpg|left|200px]]<br /><applet load="1nos" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1nos.jpg|left|200px]]<br /><applet load="1nos" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1nos, resolution 2.1&Aring;" />
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'''MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114), IMIDAZOLE COMPLEX'''<br />
'''MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114), IMIDAZOLE COMPLEX'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1NOS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with HEM and IMD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NOS OCA].  
1NOS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOS OCA].  


==Reference==
==Reference==
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[[Category: Nitric-oxide synthase]]
[[Category: Nitric-oxide synthase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Arvai, A.S.]]
[[Category: Arvai, A S.]]
[[Category: Crane, B.R.]]
[[Category: Crane, B R.]]
[[Category: Getzoff, E.D.]]
[[Category: Getzoff, E D.]]
[[Category: Stuehr, D.J.]]
[[Category: Stuehr, D J.]]
[[Category: Tainer, J.A.]]
[[Category: Tainer, J A.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: IMD]]
[[Category: IMD]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


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