1h5u

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Revision as of 05:48, 28 April 2021

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

Structural highlights

1h5u is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1a8i, 1abb, 1axr, 1b4d, 1bx3, 1c50, 1c8k, 1c8l, 1e1y, 1fs4, 1ftq, 1ftw, 1fty, 1fu4, 1fu7, 1fu8, 1gfz, 1gg8, 1ggn, 1gpa, 1gpb, 1gpy, 1hlf, 1noi, 1noj, 1nok, 1pyg, 2amv, 2gpa, 2gpb, 2gpn, 2pri, 2prj, 2skc, 2skd, 2ske, 3amv, 3gpb, 4gpb, 5gpb, 6gpb, 7gpb, 8gpb, 9gpb
Activity:	Phosphorylase, with EC number 2.4.1.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Oikonomakos NG, Zographos SE, Skamnaki VT, Archontis G. The 1.76 A resolution crystal structure of glycogen phosphorylase B complexed with glucose, and CP320626, a potential antidiabetic drug. Bioorg Med Chem. 2002 May;10(5):1313-9. PMID:11886794

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h5u"

@@ Line 3: / Line 3: @@
 <StructureSection load='1h5u' size='340' side='right'caption='[[1h5u]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[1h5u]] 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=1H5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H5U FirstGlance]. <br>
-</td></tr><tr id='ligand'><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></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
-<tr id='related'><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>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[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]]</div></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'>[https://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [https://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=1h5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5u OCA], [http://pdbe.org/1h5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h5u RCSB], [http://www.ebi.ac.uk/pdbsum/1h5u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5u 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=1h5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5u OCA], [https://pdbe.org/1h5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h5u RCSB], [https://www.ebi.ac.uk/pdbsum/1h5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5u ProSAT]</span></td></tr>
 </table>
 == 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1h5u

From Proteopedia

Revision as of 05:48, 28 April 2021

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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