4nos: Difference between revisions

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[[Image:4nos.~~gif~~|left|200px]]

[[Image:4nos.png|left|200px]]

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~~'''~~HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE WITH INHIBITOR~~'''~~

===HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE WITH INHIBITOR===

~~==Overview==~~

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Crystal structures of human endothelial nitric oxide synthase (eNOS) and human inducible NOS (iNOS) catalytic domains were solved in complex with the arginine substrate and an inhibitor S-ethylisothiourea (SEITU), respectively. The small molecules bind in a narrow cleft within the larger active-~~site cavity containing heme and tetrahydrobiopterin. Both are hydrogen~~-~~bonded to a conserved glutamate (eNOS E361, iNOS E377).~~ The ~~active-site residues of iNOS and eNOS are nearly identical. Nevertheless~~, ~~structural comparisons provide a basis for design of isozyme-selective inhibitors. The high-resolution~~, ~~refined structures of eNOS~~ (2.~~4 A resolution) and iNOS (2~~.~~25 A resolution~~) ~~reveal an unexpected structural zinc situated at~~ the ~~intermolecular interface and coordinated by four cysteines, two from each monomer~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10074942}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10074942 is the PubMed ID number.

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==About this Structure==

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[[Category: Nitric oxide]]

[[Category: Zns4]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May~~ ~~4 22~~:27:12 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:45:04 2008''

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-[[Image:4nos.gif|left|200px]]
+{{Seed}}
+[[Image:4nos.png|left|200px]]
 <!--
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 {{STRUCTURE_4nos|  PDB=4nos  |  SCENE=  }}
-'''HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE WITH INHIBITOR'''
+===HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE WITH INHIBITOR===
-==Overview==
+<!--
-Crystal structures of human endothelial nitric oxide synthase (eNOS) and human inducible NOS (iNOS) catalytic domains were solved in complex with the arginine substrate and an inhibitor S-ethylisothiourea (SEITU), respectively. The small molecules bind in a narrow cleft within the larger active-site cavity containing heme and tetrahydrobiopterin. Both are hydrogen-bonded to a conserved glutamate (eNOS E361, iNOS E377). The active-site residues of iNOS and eNOS are nearly identical. Nevertheless, structural comparisons provide a basis for design of isozyme-selective inhibitors. The high-resolution, refined structures of eNOS (2.4 A resolution) and iNOS (2.25 A resolution) reveal an unexpected structural zinc situated at the intermolecular interface and coordinated by four cysteines, two from each monomer.
+The line below this paragraph, {{ABSTRACT_PUBMED_10074942}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10074942 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10074942}}
 ==About this Structure==
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 [[Category: Nitric oxide]]
 [[Category: Zns4]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:27:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 13:45:04 2008''