5o52: Difference between revisions
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==Glycogen Phosphorylase b in complex with 33b== | ==Glycogen Phosphorylase b in complex with 33b== | ||
<StructureSection load='5o52' size='340' side='right' caption='[[5o52]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5o52' size='340' side='right'caption='[[5o52]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5o52]] 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=5O52 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5o52]] 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=5O52 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5O52 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9LE:(2~{R},3~{S},4~{R},5~{R},6~{R})-5-azanyl-2-(hydroxymethyl)-6-(4-naphthalen-2-yl-1~{H}-imidazol-2-yl)oxane-3,4-diol'>9LE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9LE:(2~{R},3~{S},4~{R},5~{R},6~{R})-5-azanyl-2-(hydroxymethyl)-6-(4-naphthalen-2-yl-1~{H}-imidazol-2-yl)oxane-3,4-diol'>9LE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5o50|5o50]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5o50|5o50]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5o52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o52 OCA], [http://pdbe.org/5o52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o52 RCSB], [http://www.ebi.ac.uk/pdbsum/5o52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o52 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5o52" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5o52" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[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 15:17, 26 August 2020
Glycogen Phosphorylase b in complex with 33bGlycogen Phosphorylase b in complex with 33b
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. Publication Abstract from PubMedAryl substituted 1-(beta-D-glucosaminyl)-1,2,3-triazoles as well as C-beta-D-glucosaminyl 1,2,4-triazoles and imidazoles were synthesized and tested as inhibitors against muscle and liver isoforms of glycogen phosphorylase (GP). While the N-beta-D-glucosaminyl 1,2,3-triazoles showed weak or no inhibition, the C-beta-D-glucosaminyl derivatives had potent activity and the best inhibitor was the 2-(beta-D-glucosaminyl)-4(5)-(2-naphthyl)-imidazole with a Ki value of 143 nM against human liver GPa. An X-ray crystallography study of the rabbit muscle GPb inhibitor complexes revealed structural features of the strong binding, and offered an explanation for the differences in inhibitory potency between glucosyl and glucosaminyl derivatives and also for the differences between imidazole and 1,2,4-triazole analogues. Nanomolar inhibitors of glycogen phosphorylase based on beta-D-glucosaminyl heterocycles: a combined synthetic, enzyme kinetic and protein crystallography study.,Bokor E, Kyriakis E, Solovou TG, Koppany C, Kantsadi AL, Szabo KE, Szakacs A, Stravodimos GA, Docsa T, Skamnaki VT, Zographos SE, Gergely P, Leonidas DD, Somsak L J Med Chem. 2017 Sep 19. doi: 10.1021/acs.jmedchem.7b01056. PMID:28925695[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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