3nos

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{{STRUCTURE_3nos| PDB=3nos | SCENE= }}
{{STRUCTURE_3nos| PDB=3nos | SCENE= }}
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'''HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE WITH ARGININE SUBSTRATE'''
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===HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE WITH ARGININE SUBSTRATE===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10074942 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10074942}}
==About this Structure==
==About this Structure==
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[[Category: Nitric oxide]]
[[Category: Nitric oxide]]
[[Category: Zns4]]
[[Category: Zns4]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:08:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 12:57:49 2008''

Revision as of 09:57, 3 July 2008

Template:STRUCTURE 3nos

HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE WITH ARGININE SUBSTRATE

Template:ABSTRACT PUBMED 10074942

About this Structure

3NOS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation., Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC, Nat Struct Biol. 1999 Mar;6(3):233-42. PMID:10074942

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