1cqe: Difference between revisions
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==Overview== | ==Overview== | ||
The three-dimensional structure of prostaglandin H2 synthase-1, an | 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== | ==About this Structure== | ||
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[[Category: Prostaglandin-endoperoxide synthase]] | [[Category: Prostaglandin-endoperoxide synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Garavito, R | [[Category: Garavito, R M.]] | ||
[[Category: Loll, P | [[Category: Loll, P J.]] | ||
[[Category: Mulichak, A | [[Category: Mulichak, A M.]] | ||
[[Category: Picot, D.]] | [[Category: Picot, D.]] | ||
[[Category: BOG]] | [[Category: BOG]] | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
''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 12:08:42 2008'' | ||
Revision as of 13:08, 21 February 2008
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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 with , and as ligands. Active as Prostaglandin-endoperoxide synthase, with EC number 1.14.99.1 Known structural/functional Sites: , , and . 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
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