1cqe: Difference between revisions
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'''PROSTAGLANDIN H2 SYNTHASE-1 COMPLEX WITH FLURBIPROFEN''' | '''PROSTAGLANDIN H2 SYNTHASE-1 COMPLEX WITH FLURBIPROFEN''' | ||
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[[Category: Mulichak, A M.]] | [[Category: Mulichak, A M.]] | ||
[[Category: Picot, D.]] | [[Category: Picot, D.]] | ||
[[Category: | [[Category: Dioxygenase]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Peroxidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:00:09 2008'' | |||
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Revision as of 13:00, 2 May 2008
PROSTAGLANDIN H2 SYNTHASE-1 COMPLEX WITH FLURBIPROFEN
OverviewOverview
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 StructureAbout this Structure
1CQE is a Single protein structure of sequence from Ovis aries. Full crystallographic information is available from OCA.
ReferenceReference
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 Fri May 2 13:00:09 2008