1prh

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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1prh ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1prh ConSurf].
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:8121489</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1prh" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[Cyclooxygenase 3D structures|Cyclooxygenase 3D structures]]
*[[Cyclooxygenase 3D structures|Cyclooxygenase 3D structures]]
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 05:33, 5 June 2024

THE X-RAY CRYSTAL STRUCTURE OF THE MEMBRANE PROTEIN PROSTAGLANDIN H2 SYNTHASE-1

PDB ID 1prh

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