5ikv: Difference between revisions

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'''Unreleased structure'''


The entry 5ikv is ON HOLD
==The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2==
 
<StructureSection load='5ikv' size='340' side='right' caption='[[5ikv]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5ikv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IKV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IKV FirstGlance]. <br>
Description:  
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=COH:PROTOPORPHYRIN+IX+CONTAINING+CO'>COH</scene>, <scene name='pdbligand=FLF:2-[[3-(TRIFLUOROMETHYL)PHENYL]AMINO]+BENZOIC+ACID'>FLF</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ikr|5ikr]], [[5ikq|5ikq]], [[5ikt|5ikt]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prostaglandin-endoperoxide_synthase Prostaglandin-endoperoxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.1 1.14.99.1] </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=5ikv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ikv OCA], [http://pdbe.org/5ikv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ikv RCSB], [http://www.ebi.ac.uk/pdbsum/5ikv PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/PGH2_HUMAN PGH2_HUMAN]] Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Constitutively expressed in some tissues in physiological conditions, such as the endothelium, kidney and brain, and in pathological conditions, such as in cancer. PTGS2 is responsible for production of inflammatory prostaglandins. Up-regulation of PTGS2 is also associated with increased cell adhesion, phenotypic changes, resistance to apoptosis and tumor angiogenesis. In cancer cells, PTGS2 is a key step in the production of prostaglandin E2 (PGE2), which plays important roles in modulating motility, proliferation and resistance to apoptosis.<ref>PMID:16373578</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Prostaglandin-endoperoxide synthase]]
[[Category: Malkowski, M G]]
[[Category: Orlando, B J]]
[[Category: Cox flufenamic]]
[[Category: Oxidoreductase]]

Revision as of 02:00, 2 June 2016

The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2

Structural highlights

5ikv is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , ,
Activity:Prostaglandin-endoperoxide synthase, with EC number 1.14.99.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PGH2_HUMAN] Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Constitutively expressed in some tissues in physiological conditions, such as the endothelium, kidney and brain, and in pathological conditions, such as in cancer. PTGS2 is responsible for production of inflammatory prostaglandins. Up-regulation of PTGS2 is also associated with increased cell adhesion, phenotypic changes, resistance to apoptosis and tumor angiogenesis. In cancer cells, PTGS2 is a key step in the production of prostaglandin E2 (PGE2), which plays important roles in modulating motility, proliferation and resistance to apoptosis.[1]

References

  1. ↑ Kim SF, Huri DA, Snyder SH. Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2. Science. 2005 Dec 23;310(5756):1966-70. PMID:16373578 doi:http://dx.doi.org/10.1126/science.1119407

5ikv, resolution 2.51Å

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