1dd0

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1dd0.png|left|200px]]
 
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==MOLECULAR MODEL OF PROSTAGLANDIN G2 BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF COX-2==
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The line below this paragraph, containing "STRUCTURE_1dd0", creates the "Structure Box" on the page.
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<StructureSection load='1dd0' size='340' side='right'caption='[[1dd0]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DD0 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dd0 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1dd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dd0 ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1dd0| PDB=1dd0 | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cyclooxygenases are bifunctional enzymes that catalyse the first committed step in the synthesis of prostaglandins, thromboxanes and other eicosanoids. The two known cyclooxygenases isoforms share a high degree of amino-acid sequence similarity, structural topology and an identical catalytic mechanism. Cyclooxygenase enzymes catalyse two sequential reactions in spatially distinct, but mechanistically coupled active sites. The initial cyclooxygenase reaction converts arachidonic acid (which is achiral) to prostaglandin G2 (which has five chiral centres). The subsequent peroxidase reaction reduces prostaglandin G2 to prostaglandin H2. Here we report the co-crystal structures of murine apo-cyclooxygenase-2 in complex with arachidonic acid and prostaglandin. These structures suggest the molecular basis for the stereospecificity of prostaglandin G2 synthesis.
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===MOLECULAR MODEL OF PROSTAGLANDIN G2 BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF COX-2===
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Structural insights into the stereochemistry of the cyclooxygenase reaction.,Kiefer JR, Pawlitz JL, Moreland KT, Stegeman RA, Hood WF, Gierse JK, Stevens AM, Goodwin DC, Rowlinson SW, Marnett LJ, Stallings WC, Kurumbail RG Nature. 2000 May 4;405(6782):97-101. PMID:10811226<ref>PMID:10811226</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>
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The line below this paragraph, {{ABSTRACT_PUBMED_10811226}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1dd0" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10811226 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10811226}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD0 OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:10811226</ref><references group="xtra"/>
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[[Category: Gierse, J K]]
[[Category: Gierse, J K]]
[[Category: Goodwin, D C]]
[[Category: Goodwin, D C]]
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[[Category: Stegeman, R A]]
[[Category: Stegeman, R A]]
[[Category: Stevens, A M]]
[[Category: Stevens, A M]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 07:19:34 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MOLECULAR MODEL OF PROSTAGLANDIN G2 BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF COX-2

PDB ID 1dd0

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