1h5u

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[[Image:1h5u.png|left|200px]]
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==THE 1.76 A RESOLUTION CRYSTAL STRUCTURE OF GLYCOGEN PHOSPHORYLASE B COMPLEXED WITH GLUCOSE AND CP320626, A POTENTIAL ANTIDIABETIC DRUG==
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<StructureSection load='1h5u' size='340' side='right' caption='[[1h5u]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1h5u]] 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=1H5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H5U FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHI:5-CHLORO-1H-INDOLE-2-CARBOXYLIC+ACID+[1-(4-FLUOROBENZYL)-2-(4-HYDROXYPIPERIDIN-1YL)-2-OXOETHYL]AMIDE'>CHI</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a8i|1a8i]], [[1abb|1abb]], [[1axr|1axr]], [[1b4d|1b4d]], [[1bx3|1bx3]], [[1c50|1c50]], [[1c8k|1c8k]], [[1c8l|1c8l]], [[1e1y|1e1y]], [[1fs4|1fs4]], [[1ftq|1ftq]], [[1ftw|1ftw]], [[1fty|1fty]], [[1fu4|1fu4]], [[1fu7|1fu7]], [[1fu8|1fu8]], [[1gfz|1gfz]], [[1gg8|1gg8]], [[1ggn|1ggn]], [[1gpa|1gpa]], [[1gpb|1gpb]], [[1gpy|1gpy]], [[1hlf|1hlf]], [[1noi|1noi]], [[1noj|1noj]], [[1nok|1nok]], [[1pyg|1pyg]], [[2amv|2amv]], [[2gpa|2gpa]], [[2gpb|2gpb]], [[2gpn|2gpn]], [[2pri|2pri]], [[2prj|2prj]], [[2skc|2skc]], [[2skd|2skd]], [[2ske|2ske]], [[3amv|3amv]], [[3gpb|3gpb]], [[4gpb|4gpb]], [[5gpb|5gpb]], [[6gpb|6gpb]], [[7gpb|7gpb]], [[8gpb|8gpb]], [[9gpb|9gpb]]</td></tr>
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<tr><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>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h5u RCSB], [http://www.ebi.ac.uk/pdbsum/1h5u PDBsum]</span></td></tr>
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<table>
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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/h5/1h5u_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/chain_selection.php?pdb_ID=2ata 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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CP320626, a potential antidiabetic drug, inhibits glycogen phosphorylase in synergism with glucose. To elucidate the structural basis of synergistic inhibition, we determined the structure of muscle glycogen phosphorylase b (MGPb) complexed with both glucose and CP320626 at 1.76 A resolution, and refined to a crystallographic R value of 0.211 (R(free)=0.235). CP320626 binds at a novel allosteric site, which is some 33 A from the catalytic site, where glucose binds. The high resolution structure allows unambiguous definition of the conformation of the 1-acetyl-4-hydroxy-piperidine ring supported by theoretical energy calculations. Both CP320626 and glucose promote the less active T-state, thereby explaining their synergistic inhibition. Structural comparison of MGPb--glucose--CP320626 complex with liver glycogen phosphorylase a (LGPa) complexed with a related compound (CP403700) show that the ligand binding site is conserved in LGPa.
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{{STRUCTURE_1h5u| PDB=1h5u | SCENE= }}
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The 1.76 A resolution crystal structure of glycogen phosphorylase B complexed with glucose, and CP320626, a potential antidiabetic drug.,Oikonomakos NG, Zographos SE, Skamnaki VT, Archontis G Bioorg Med Chem. 2002 May;10(5):1313-9. PMID:11886794<ref>PMID:11886794</ref>
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===THE 1.76 A RESOLUTION CRYSTAL STRUCTURE OF GLYCOGEN PHOSPHORYLASE B COMPLEXED WITH GLUCOSE AND CP320626, A POTENTIAL ANTIDIABETIC DRUG===
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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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{{ABSTRACT_PUBMED_11886794}}
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==About this Structure==
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[[1h5u]] 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=1H5U OCA].
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==See Also==
==See Also==
*[[Glycogen Phosphorylase|Glycogen Phosphorylase]]
*[[Glycogen Phosphorylase|Glycogen Phosphorylase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:011886794</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Phosphorylase]]
[[Category: Phosphorylase]]

Revision as of 14:22, 28 September 2014

THE 1.76 A RESOLUTION CRYSTAL STRUCTURE OF GLYCOGEN PHOSPHORYLASE B COMPLEXED WITH GLUCOSE AND CP320626, A POTENTIAL ANTIDIABETIC DRUG

1h5u, resolution 1.76Å

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