5o50: Difference between revisions
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==Glycogen Phosphorylase b in complex with 33a== | ==Glycogen Phosphorylase b in complex with 33a== | ||
<StructureSection load='5o50' size='340' side='right' caption='[[5o50]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5o50' size='340' side='right'caption='[[5o50]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5o50]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5o50]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O50 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9L2:(2~{R},3~{S},4~{R},5~{R},6~{R})-5-azanyl-2-(hydroxymethyl)-6-(4-phenyl-1~{H}-imidazol-2-yl)oxane-3,4-diol'>9L2</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9L2:(2~{R},3~{S},4~{R},5~{R},6~{R})-5-azanyl-2-(hydroxymethyl)-6-(4-phenyl-1~{H}-imidazol-2-yl)oxane-3,4-diol'>9L2</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=5o50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o50 OCA], [https://pdbe.org/5o50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o50 RCSB], [https://www.ebi.ac.uk/pdbsum/5o50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o50 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PYGM_RABIT 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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 19: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5o50" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5o50" 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: Chatzileontiadou DS]] | |||
[[Category: Chatzileontiadou | [[Category: Kantsadi AL]] | ||
[[Category: Kantsadi | [[Category: Kyriakis E]] | ||
[[Category: Kyriakis | [[Category: Leonidas DD]] | ||
[[Category: Leonidas | [[Category: Skamnaki VT]] | ||
[[Category: Skamnaki | [[Category: Solovou TGA]] | ||
[[Category: Solovou | [[Category: Stravodimos GA]] | ||
[[Category: Stravodimos | |||
Latest revision as of 22:08, 29 November 2023
Glycogen Phosphorylase b in complex with 33aGlycogen Phosphorylase b in complex with 33a
Structural highlights
FunctionPYGM_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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