Sandbox Reserved 1471

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== Function ==
== Function ==
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== Structure ==
== Structure ==
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== Energetics ==
== Energetics ==
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== Medical Applications ==
== Medical Applications ==
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== Comparison between the Isozymes Cyclooxygenase 1 and Cyclooxygenase 2 ==
== Comparison between the Isozymes Cyclooxygenase 1 and Cyclooxygenase 2 ==
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</StructureSection>
 
== References ==
== References ==
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<references/>

Revision as of 22:26, 3 December 2018

This Sandbox is Reserved from November 5 2018 through January 1, 2019 for use in the course "CHEM 4923: Senior Project taught by Christina R. Bourne at the University of Oklahoma, Norman, USA. This reservation includes Sandbox Reserved 1471 through Sandbox Reserved 1478.
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Contents

Cyclooxygenase 2

Human Cyclooxygenase 2 bound to Rofecoxib. PDB file 5KIR.

Drag the structure with the mouse to rotate

Background

Cyclooxygenases are enzymes that catalyze the transformation of arachidonic acid into prostaglandins, prostacyclins, and thromboxanes.[1] Another name for cyclooxygenases is prostaglandin H2 synthase. There are two names because there are two catalytic activities: cyclooxygenase and peroxidase. The abbreviation for cyclooxygenase and prostaglandin H2 synthase is COX and PGHS respectively and can be used interchangeably. There are two types of cyclooxygenases: COX-1 and COX-2. COX-1 is responsible for platelet aggregation and gastric acidity.[1] COX-2 is involved in pathways that lead to inflammation (swelling), pain, and fever.[1]

Function

Structure

Energetics

Medical Applications

Comparison between the Isozymes Cyclooxygenase 1 and Cyclooxygenase 2

References

  1. ↑ 1.0 1.1 1.2 Orlando BJ, Malkowski MG. Crystal structure of rofecoxib bound to human cyclooxygenase-2. Acta Crystallogr F Struct Biol Commun. 2016 Oct 1;72(Pt 10):772-776. Epub 2016, Sep 22. PMID:27710942 doi:http://dx.doi.org/10.1107/S2053230X16014230
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