1dqa: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1dqa.gif|left|200px]]<br /><applet load="1dqa" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1dqa.gif|left|200px]]
caption="1dqa, resolution 2.00&Aring;" />
 
'''COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH HMG, COA, AND NADP+'''<br />
{{Structure
|PDB= 1dqa |SIZE=350|CAPTION= <scene name='initialview01'>1dqa</scene>, resolution 2.00&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MAH:3-HYDROXY-3-METHYL-GLUTARIC+ACID'>MAH</scene> and <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Hydroxymethylglutaryl-CoA_reductase_(NADPH) Hydroxymethylglutaryl-CoA reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.34 1.1.1.34]
|GENE=
}}
 
'''COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH HMG, COA, AND NADP+'''
 


==Overview==
==Overview==
Line 10: Line 19:


==About this Structure==
==About this Structure==
1DQA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=COA:'>COA</scene>, <scene name='pdbligand=MAH:'>MAH</scene> and <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hydroxymethylglutaryl-CoA_reductase_(NADPH) Hydroxymethylglutaryl-CoA reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.34 1.1.1.34] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQA OCA].  
1DQA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQA OCA].  


==Reference==
==Reference==
Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis., Istvan ES, Palnitkar M, Buchanan SK, Deisenhofer J, EMBO J. 2000 Mar 1;19(5):819-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10698924 10698924]
Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis., Istvan ES, Palnitkar M, Buchanan SK, Deisenhofer J, EMBO J. 2000 Mar 1;19(5):819-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10698924 10698924]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Hydroxymethylglutaryl-CoA reductase (NADPH)]]
[[Category: Hydroxymethylglutaryl-CoA reductase (NADPH)]]
Line 29: Line 38:
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:20 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:42:35 2008''

Revision as of 11:42, 20 March 2008

File:1dqa.gif


PDB ID 1dqa

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , and
Activity: Hydroxymethylglutaryl-CoA reductase (NADPH), with EC number 1.1.1.34
Coordinates: save as pdb, mmCIF, xml



COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH HMG, COA, AND NADP+


OverviewOverview

3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes the formation of mevalonate, the committed step in the biosynthesis of sterols and isoprenoids. The activity of HMGR is controlled through synthesis, degradation and phosphorylation to maintain the concentration of mevalonate-derived products. In addition to the physiological regulation of HMGR, the human enzyme has been targeted successfully by drugs in the clinical treatment of high serum cholesterol levels. Three crystal structures of the catalytic portion of human HMGR in complexes with HMG-CoA, with HMG and CoA, and with HMG, CoA and NADP(+), provide a detailed view of the enzyme active site. Catalytic portions of human HMGR form tight tetramers. The crystal structure explains the influence of the enzyme's oligomeric state on the activity and suggests a mechanism for cholesterol sensing. The active site architecture of human HMGR is different from that of bacterial HMGR; this may explain why binding of HMGR inhibitors to bacterial HMGRs has not been reported.

DiseaseDisease

Known disease associated with this structure: Statins, attenuated cholesterol lowering by OMIM:[142910]

About this StructureAbout this Structure

1DQA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis., Istvan ES, Palnitkar M, Buchanan SK, Deisenhofer J, EMBO J. 2000 Mar 1;19(5):819-30. PMID:10698924

Page seeded by OCA on Thu Mar 20 10:42:35 2008

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

OCA