1cqe: Difference between revisions
No edit summary |
No edit summary |
||
Line 7: | Line 7: | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cqe RCSB], [http://www.ebi.ac.uk/pdbsum/1cqe PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cqe RCSB], [http://www.ebi.ac.uk/pdbsum/1cqe PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/PGH1_SHEEP PGH1_SHEEP]] May play an important role in regulating or promoting cell proliferation in some normal and neoplastically transformed cells. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 22:08, 25 December 2014
PROSTAGLANDIN H2 SYNTHASE-1 COMPLEX WITH FLURBIPROFENPROSTAGLANDIN H2 SYNTHASE-1 COMPLEX WITH FLURBIPROFEN
Structural highlights
Function[PGH1_SHEEP] May play an important role in regulating or promoting cell proliferation in some normal and neoplastically transformed cells. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|