6r0h
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Glycogen Phosphorylase b in complex with 3== | |
| + | <StructureSection load='6r0h' size='340' side='right'caption='[[6r0h]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6r0h]] 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=6R0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R0H FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=JN2:3-(4-fluorophenyl)-~{N}-[(2~{R},3~{R},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]benzamide'>JN2</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'>[https://proteopedia.org/fgij/fg.htm?mol=6r0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r0h OCA], [https://pdbe.org/6r0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r0h RCSB], [https://www.ebi.ac.uk/pdbsum/6r0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r0h ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Structure-based design and synthesis of two biphenyl-N-acyl-beta-d-glucopyranosylamine derivatives as well as their assessment as inhibitors of human liver glycogen phosphorylase (hlGPa, a pharmaceutical target for type 2 diabetes) is presented. X-ray crystallography revealed the importance of structural water molecules and that the inhibitory efficacy correlates with the degree of disturbance caused by the inhibitor binding to a loop crucial for the catalytic mechanism. The in silico-derived models of the binding mode generated during the design process corresponded very well with the crystallographic data. | ||
| - | + | High Consistency of Structure-Based Design and X-Ray Crystallography: Design, Synthesis, Kinetic Evaluation and Crystallographic Binding Mode Determination of Biphenyl-N-acyl-beta-d-Glucopyranosylamines as Glycogen Phosphorylase Inhibitors.,Fischer T, Koulas SM, Tsagkarakou AS, Kyriakis E, Stravodimos GA, Skamnaki VT, Liggri PGV, Zographos SE, Riedl R, Leonidas DD Molecules. 2019 Apr 3;24(7). pii: molecules24071322. doi:, 10.3390/molecules24071322. PMID:30987252<ref>PMID:30987252</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6r0h" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Leonidas | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Stravodimos | + | [[Category: Large Structures]] |
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: Koulas MS]] | ||
| + | [[Category: Kyriakis E]] | ||
| + | [[Category: Leonidas DD]] | ||
| + | [[Category: Skamnaki VT]] | ||
| + | [[Category: Stravodimos GA]] | ||
| + | [[Category: Tsagkarakou SA]] | ||
Current revision
Glycogen Phosphorylase b in complex with 3
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