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| | ==Glycogen phosphorylase in complex with chlorogenic acid.== | | ==Glycogen phosphorylase in complex with chlorogenic acid.== |
| - | <StructureSection load='5mcb' size='340' side='right' caption='[[5mcb]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='5mcb' size='340' side='right'caption='[[5mcb]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5mcb]] 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=5MCB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MCB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mcb]] 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=5MCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MCB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CGG:Chlorogenic+acid'>CGG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CGG:Chlorogenic+acid'>CGG</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5mcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mcb OCA], [http://pdbe.org/5mcb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mcb RCSB], [http://www.ebi.ac.uk/pdbsum/5mcb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mcb ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mcb OCA], [https://pdbe.org/5mcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mcb RCSB], [https://www.ebi.ac.uk/pdbsum/5mcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mcb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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 == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5mcb" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5mcb" 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: Chatzileontiadou DSM]] |
| - | [[Category: Chatzileontiadou, D S.M]] | + | [[Category: Kantsadi AL]] |
| - | [[Category: Kantsadi, A L]] | + | [[Category: Kyriakis E]] |
| - | [[Category: Kyriakis, E]] | + | [[Category: Leonidas DD]] |
| - | [[Category: Leonidas, D D]] | + | [[Category: Stravodimos GA]] |
| - | [[Category: Stravodimos, G A]] | + | |
| - | [[Category: Alpha and beta protein]]
| + | |
| - | [[Category: Transferase]]
| + | |
| 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 PubMed
BACKGROUND: Glycogen phosphorylase (GP) is a pharmaceutical target for the discovery of new antihyperglycaemic agents. Punica granatum is a well-known plant for its potent antioxidant and antimicrobial activities but so far has not been examined for antihyperglycaemic activity. OBJECTIVE: To examine the inhibitory potency of eighteen polyphenolic extracts obtained from Punica granatum fruits and industrial juicing byproducts against GP and discover their most bioactive ingredients. METHOD: Kinetic experiments were conducted to measure the IC50 values of the extracts while affinity crystallography was used to identify the most bioactive ingredient. The inhibitory effect of one of the polyphenolic extracts was also verified ex vivo, in HepG2 cells. RESULTS: All extracts exhibit significant in vitro inhibitory potency (IC50 values in the range of low mug/mL). Affinity crystallography revealed that the most bioactive ingredients of the extracts were chlorogenic and ellagic acids, found bound in the active and the inhibitor site of GP, respectively. While ellagic acid is an established GP inhibitor, the inhibition of chlorogenic acid is reported for the first time. Kinetic analysis indicated that chlorogenic acid is an inhibitor with Ki=2.5 x 10-3 M that acts synergistically with ellagic acid. CONCLUSION: Our study provides the first evidence for a potential antidiabetic usage of Punica granatum extracts as antidiabetic food supplements. Although, more in vivo studies have to be performed before these extracts reach the stage of antidiabetic food supplements our study provides a first positive step towards this process.
Affinity crystallography reveals the bioactive compounds of industrial juicing byproducts of Punica granatum for glycogen phosphorylase.,Stravodimos GA, Kantsadi AL, Apostolou A, Kyriakis E, Kafaski-Kanelli VN, Solovou TGA, Gatzona P, Liggri PC, Theofanous S, Gorgogietas VA, Kissa A, Psachoula C, Chatzileontiadou DSM, Lemonakis A, Psarra AG, Skamnaki VT, Haroutounian S, Leonidas DD Curr Drug Discov Technol. 2017 Jun 18. doi: 10.2174/1570163814666170619091736. PMID:28625148[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stravodimos GA, Kantsadi AL, Apostolou A, Kyriakis E, Kafaski-Kanelli VN, Solovou TGA, Gatzona P, Liggri PC, Theofanous S, Gorgogietas VA, Kissa A, Psachoula C, Chatzileontiadou DSM, Lemonakis A, Psarra AG, Skamnaki VT, Haroutounian S, Leonidas DD. Affinity crystallography reveals the bioactive compounds of industrial juicing byproducts of Punica granatum for glycogen phosphorylase. Curr Drug Discov Technol. 2017 Jun 18. doi: 10.2174/1570163814666170619091736. PMID:28625148 doi:http://dx.doi.org/10.2174/1570163814666170619091736
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