2gm9: Difference between revisions
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==Structure of rabbit muscle glycogen phosphorylase in complex with thienopyrrole== | ==Structure of rabbit muscle glycogen phosphorylase in complex with thienopyrrole== | ||
<StructureSection load='2gm9' size='340' side='right' caption='[[2gm9]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2gm9' size='340' side='right' caption='[[2gm9]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gj4|2gj4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gj4|2gj4]]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gm9 OCA], [http://pdbe.org/2gm9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gm9 RCSB], [http://www.ebi.ac.uk/pdbsum/2gm9 PDBsum]</span></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=2gm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gm9 OCA], [http://pdbe.org/2gm9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gm9 RCSB], [http://www.ebi.ac.uk/pdbsum/2gm9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gm9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gm/2gm9_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gm/2gm9_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:02, 20 June 2018
Structure of rabbit muscle glycogen phosphorylase in complex with thienopyrroleStructure of rabbit muscle glycogen phosphorylase in complex with thienopyrrole
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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTwo series of novel thienopyrrole inhibitors of recombinant human liver glycogen phosphorylase a (GPa) which are effective in reducing glucose output from rat hepatocytes are described. Representative compounds have been shown to bind at the dimer interface site of the rabbit muscle enzyme by X-ray crystallography. Novel thienopyrrole glycogen phosphorylase inhibitors: synthesis, in vitro SAR and crystallographic studies.,Whittamore PR, Addie MS, Bennett SN, Birch AM, Butters M, Godfrey L, Kenny PW, Morley AD, Murray PM, Oikonomakos NG, Otterbein LR, Pannifer AD, Parker JS, Readman K, Siedlecki PS, Schofield P, Stocker A, Taylor MJ, Townsend LA, Whalley DP, Whitehouse J Bioorg Med Chem Lett. 2006 Nov 1;16(21):5567-71. Epub 2006 Aug 30. PMID:16945526[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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