2qn2

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{{Seed}}
 
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[[Image:2qn2.png|left|200px]]
 
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==Glycogen Phosphorylase b in complex with Maslinic Acid==
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The line below this paragraph, containing "STRUCTURE_2qn2", creates the "Structure Box" on the page.
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<StructureSection load='2qn2' size='340' side='right'caption='[[2qn2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2qn2]] 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=2QN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QN2 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.698&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0MA:MASLINIC+ACID'>0MA</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
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{{STRUCTURE_2qn2| PDB=2qn2 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qn2 OCA], [https://pdbe.org/2qn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qn2 RCSB], [https://www.ebi.ac.uk/pdbsum/2qn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qn2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/2qn2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qn2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Twenty-five naturally occurring pentacyclic triterpenes, 15 of which were synthesized in this study, were biologically evaluated as inhibitors of rabbit muscle glycogen phosphorylase a (GPa). From SAR studies, the presence of a sugar moiety in triterpene saponins resulted in a markedly decreased activity ( 7, 18- 20) or no activity ( 21, 22). These saponins, however, might find their value as potential natural prodrugs which are much more water-soluble than their corresponding aglycones. To elucidate the mechanism of GP inhibition, we have determined the crystal structures of the GPb-asiatic acid and GPb-maslinic acid complexes. The X-ray analysis indicates that the inhibitors bind at the allosteric activator site, where the physiological activator AMP binds. Pentacyclic triterpenes represent a promising class of multiple-target antidiabetic agents that exert hypoglycemic effects, at least in part, through GP inhibition.
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===Glycogen Phosphorylase b in complex with Maslinic Acid===
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Naturally occurring pentacyclic triterpenes as inhibitors of glycogen phosphorylase: synthesis, structure-activity relationships, and X-ray crystallographic studies.,Wen X, Sun H, Liu J, Cheng K, Zhang P, Zhang L, Hao J, Zhang L, Ni P, Zographos SE, Leonidas DD, Alexacou KM, Gimisis T, Hayes JM, Oikonomakos NG J Med Chem. 2008 Jun 26;51(12):3540-54. Epub 2008 Jun 3. PMID:18517260<ref>PMID:18517260</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2qn2" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18517260}}, adds the Publication Abstract to the page
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*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18517260 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18517260}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2QN2 is a 1 chain structure of 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=2QN2 OCA].
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==Reference==
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<ref group="xtra">PMID:18517260</ref><references group="xtra"/>
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Phosphorylase]]
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[[Category: Alexacou K-M]]
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[[Category: Alexacou, K M.]]
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[[Category: Hayes J]]
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[[Category: Hayes, J.]]
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[[Category: Leonidas DD]]
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[[Category: Leonidas, D D.]]
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[[Category: Oikonomakos NG]]
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[[Category: Oikonomakos, N G.]]
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[[Category: Zographos SE]]
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[[Category: Zographos, S E.]]
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[[Category: Apoptosis]]
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[[Category: Glycogenolysis]]
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[[Category: Transferase]]
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[[Category: Type 2 diabetes]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:44:35 2009''
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Current revision

Glycogen Phosphorylase b in complex with Maslinic Acid

PDB ID 2qn2

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