2gj4: Difference between revisions
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==Structure of rabbit muscle glycogen phosphorylase in complex with ligand== | ==Structure of rabbit muscle glycogen phosphorylase in complex with ligand== | ||
<StructureSection load='2gj4' size='340' side='right' caption='[[2gj4]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='2gj4' size='340' side='right'caption='[[2gj4]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2gj4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GJ4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2gj4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GJ4 FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Glycogen | *[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Phosphorylase]] | [[Category: Phosphorylase]] |
Revision as of 14:15, 27 March 2020
Structure of rabbit muscle glycogen phosphorylase in complex with ligandStructure of rabbit muscle glycogen phosphorylase in complex with ligand
Structural highlights
Function[PYGM_RABIT] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. 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 PubMedTwo series of novel thienopyrrole inhibitors of recombinant human liver glycogen phosphorylase a (GPa) which are effective in reducing glucose output from rat hepatocytes are described. Representative compounds have been shown to bind at the dimer interface site of the rabbit muscle enzyme by X-ray crystallography. Novel thienopyrrole glycogen phosphorylase inhibitors: synthesis, in vitro SAR and crystallographic studies.,Whittamore PR, Addie MS, Bennett SN, Birch AM, Butters M, Godfrey L, Kenny PW, Morley AD, Murray PM, Oikonomakos NG, Otterbein LR, Pannifer AD, Parker JS, Readman K, Siedlecki PS, Schofield P, Stocker A, Taylor MJ, Townsend LA, Whalley DP, Whitehouse J Bioorg Med Chem Lett. 2006 Nov 1;16(21):5567-71. Epub 2006 Aug 30. PMID:16945526[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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