1hwl: Difference between revisions
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<StructureSection load='1hwl' size='340' side='right'caption='[[1hwl]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1hwl' size='340' side='right'caption='[[1hwl]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hwl]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWL OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[1hwl]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HWL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FBI:7-[4-(4-FLUORO-PHENYL)-6-ISOPROPYL-2-(METHANESULFONYL-METHYL-AMINO)-PYRIMIDIN-5-YL]+-3,5-DIHYDROXY-HEPTANOIC+ACID'>FBI</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FBI:7-[4-(4-FLUORO-PHENYL)-6-ISOPROPYL-2-(METHANESULFONYL-METHYL-AMINO)-PYRIMIDIN-5-YL]+-3,5-DIHYDROXY-HEPTANOIC+ACID'>FBI</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dq8|1dq8]], [[1dq9|1dq9]], [[1dqa|1dqa]], [[1hw8|1hw8]], [[1hw9|1hw9]], [[1hwi|1hwi]], [[1hwj|1hwj]], [[1hwk|1hwk]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dq8|1dq8]], [[1dq9|1dq9]], [[1dqa|1dqa]], [[1hw8|1hw8]], [[1hw9|1hw9]], [[1hwi|1hwi]], [[1hwj|1hwj]], [[1hwk|1hwk]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydroxymethylglutaryl-CoA_reductase_(NADPH) Hydroxymethylglutaryl-CoA reductase (NADPH)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.34 1.1.1.34] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hwl OCA], [https://pdbe.org/1hwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hwl RCSB], [https://www.ebi.ac.uk/pdbsum/1hwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hwl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/HMDH_HUMAN HMDH_HUMAN]] Transmembrane glycoprotein that is the rate-limiting enzyme in cholesterol biosynthesis as well as in the biosynthesis of nonsterol isoprenoids that are essential for normal cell function including ubiquinone and geranylgeranyl proteins. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[HMG-CoA Reductase|HMG-CoA Reductase]] | *[[HMG-CoA Reductase|HMG-CoA Reductase]] | ||
*[[HMG-CoA Reductase 3D structures|HMG-CoA Reductase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:29, 7 April 2021
COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH ROSUVASTATIN (FORMALLY KNOWN AS ZD4522)COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH ROSUVASTATIN (FORMALLY KNOWN AS ZD4522)
Structural highlights
Function[HMDH_HUMAN] Transmembrane glycoprotein that is the rate-limiting enzyme in cholesterol biosynthesis as well as in the biosynthesis of nonsterol isoprenoids that are essential for normal cell function including ubiquinone and geranylgeranyl proteins. 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 PubMedHMG-CoA (3-hydroxy-3-methylglutaryl-coenzyme A) reductase (HMGR) catalyzes the committed step in cholesterol biosynthesis. Statins are HMGR inhibitors with inhibition constant values in the nanomolar range that effectively lower serum cholesterol levels and are widely prescribed in the treatment of hypercholesterolemia. We have determined structures of the catalytic portion of human HMGR complexed with six different statins. The statins occupy a portion of the binding site of HMG-CoA, thus blocking access of this substrate to the active site. Near the carboxyl terminus of HMGR, several catalytically relevant residues are disordered in the enzyme-statin complexes. If these residues were not flexible, they would sterically hinder statin binding. Structural mechanism for statin inhibition of HMG-CoA reductase.,Istvan ES, Deisenhofer J Science. 2001 May 11;292(5519):1160-4. PMID:11349148[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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