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1prh
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(New page: 200px<br /> <applet load="1prh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1prh, resolution 3.5Å" /> '''THE X-RAY CRYSTAL ST...)
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Revision as of 06:57, 18 November 2007
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THE X-RAY CRYSTAL STRUCTURE OF THE MEMBRANE PROTEIN PROSTAGLANDIN H2 SYNTHASE-1
Overview
The three-dimensional structure of prostaglandin H2 synthase-1, an, integral membrane protein, has been determined at 3.5 A resolution by, X-ray crystallography. This bifunctional enzyme comprises three, independent folding units: an epidermal growth factor domain, a, membrane-binding motif and an enzymatic domain. Two adjacent but spatially, distinct active sites were found for its haem-dependent peroxidase and, cyclooxygenase activities. The cyclooxygenase active site is created by a, long, hydrophobic channel that is the site of non-steroidal, anti-inflammatory drug binding. The conformation of the membrane-binding, motif strongly suggests that the enzyme integrates into only one leaflet, of the lipid bilayer and is thus a monotopic membrane protein.
About this Structure
1PRH is a Single protein structure of sequence from Ovis aries with HEM as ligand. The following page contains interesting information on the relation of 1PRH with [Cyclooxygenase]. Full crystallographic information is available from OCA.
Reference
The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1., Picot D, Loll PJ, Garavito RM, Nature. 1994 Jan 20;367(6460):243-9. PMID:8121489
Page seeded by OCA on Sun Nov 18 09:04:48 2007
