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3nos

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(New page: 200px<br /> <applet load="3nos" size="450" color="white" frame="true" align="right" spinBox="true" caption="3nos, resolution 2.400&Aring;" /> '''HUMAN ENDOTHELIAL ...)
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Revision as of 21:42, 12 November 2007

Image:3nos.gif

3nos, resolution 2.400Å

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HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE WITH ARGININE SUBSTRATE

Contents

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.

Disease

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], Placental abruption OMIM:[163729]

About this Structure

3NOS is a Single protein structure of sequence from Homo sapiens with ZN, HAR, HEM and H4B as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 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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