3nos: Difference between revisions
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==Overview== | ==Overview== | ||
Crystal structures of human endothelial nitric oxide synthase (eNOS) and | 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. | ||
==Disease== | ==Disease== | ||
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[[Category: Nitric-oxide synthase]] | [[Category: Nitric-oxide synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fischmann, T | [[Category: Fischmann, T O.]] | ||
[[Category: Weber, P | [[Category: Weber, P C.]] | ||
[[Category: H4B]] | [[Category: H4B]] | ||
[[Category: HAR]] | [[Category: HAR]] | ||
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[[Category: zns4]] | [[Category: zns4]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:33 2008'' | ||
Revision as of 20:10, 21 February 2008
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HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE WITH ARGININE SUBSTRATE
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Alzheimer disease, late-onset, susceptibility to OMIM:[163729], Coronary spasms, susceptibility to OMIM:[163729], Hypertension, pregnancy-induced OMIM:[163729], Hypertension, susceptibility to OMIM:[163729], Ischemic stroke, susceptibility to OMIM:[163729], Placental abruption OMIM:[163729]
About this StructureAbout this Structure
3NOS is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.
ReferenceReference
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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