Cerivastatin: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

David Canner, Alexander Berchansky

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-<applet   load="" size="480" color="" frame="true"  spin="on" Scene ="Fluvastatin/Fluvastatin/2" align="right" caption="Fluvastatin, also known as Lescol"/>
+<applet   load="" size="480" color="" frame="true"  spin="on" Scene ="Cerivastatin/Ceriv/1" align="right" caption="Cerivastatin, also known as Baycol"/>
 ===Better Known as: Baycol===
 * Marketed By: Bayer <br />
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 * The following is a list of Pharmacokinetic Parameters. See: [[Pharmaceutical Drugs]] for more information
 ===Mechanism of Action===
-Cerivastatin is an inhibitor of [[HMG-CoA Reductase]] (HMGR), a highly <scene name='Fluvastatin/Hmg/1'>regulated enzyme</scene> responsible for the committed step in cholesterol synthesis.<ref>PMID:7784310</ref> Fluvastatin, like most of the statins, <scene name='Fluvastatin/Statin_fluva/1'>binds HMGR</scene> via a number of polar interactions with the "cis loop" of HMGR, particularly residues Ser 684, Asp 690, Lys 691, Lys 692, and hydrogen bond interactions between Glu 559 and Asp 767 with the O5-hydroxyl of the statins. Van der Waals interactions between Leu 562, Val 683, Leu 853, Ala 856, and Leu 857 of HMGR and hydrophobic ring structures of Fluvastatin contribute to binding as well.<ref>PMID:11349148</ref> These interactions help Fluvastatin outcompete HMG-CoA, the substrate of HMGR, in binding to HMGR.<ref>PMID:7784310</ref>
+Cerivastatin is an inhibitor of [[HMG-CoA Reductase]] (HMGR), a highly <scene name='Cerivastatin/Chmg/1'>regulated enzyme</scene> responsible for the committed step in cholesterol synthesis.<ref>PMID:7784310</ref> Cerivastatin, like most of the statins, <scene name='Cerivastatin/Statin_ceriv/2'>binds HMGR</scene> via a number of polar interactions with the "cis loop" of HMGR, particularly residues Ser 684, Asp 690, Lys 691, Lys 692, and hydrogen bond interactions between Glu 559 and Asp 767 with the O5-hydroxyl of the statins. Van der Waals interactions between Leu 562, Val 683, Leu 853, Ala 856, and Leu 857 of HMGR and hydrophobic ring structures of Fluvastatin contribute to binding as well.<ref>PMID:11349148</ref> These interactions help Cerivastatin outcompete HMG-CoA, the substrate of HMGR, in binding to HMGR.<ref>PMID:7784310</ref>
 ===Pharmacokinetics===
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