3zcq - Revision history

OCA at 10:58, 20 December 2023

OCA — Wed, 20 Dec 2023 10:58:56 GMT

←Older revision		Revision as of 10:58, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3zcq]] 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=3ZCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZCQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[3zcq]] 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=3ZCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZCQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=62N:N-{[4-(TRIFLUOROMETHYL)BENZOYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>62N</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.15Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zcp\|3zcp]], [[3zcr\|3zcr]], [[3zcs\|3zcs]], [[3zct\|3zct]], [[3zcu\|3zcu]], [[3zcv\|3zcv]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=62N:N-{[4-(TRIFLUOROMETHYL)BENZOYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>62N</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=3zcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zcq OCA], [https://pdbe.org/3zcq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zcq RCSB], [https://www.ebi.ac.uk/pdbsum/3zcq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zcq 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=3zcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zcq OCA], [https://pdbe.org/3zcq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zcq RCSB], [https://www.ebi.ac.uk/pdbsum/3zcq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zcq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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.	+	[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 ==~~	+
-	Two substituted ureas of beta-D-glucose, N-acetyl-N'-beta-D-glucopyranosyl urea (Acurea) and N-benzoyl-N'-beta-D-glucopyranosyl urea (Bzurea), have been identified as inhibitors of glycogen phosphorylase, a potential target for therapeutic intervention in type 2 diabetes. To elucidate the structural basis of inhibition, we determined the structure of muscle glycogen phosphorylase b (GPb) complexed with the two compounds at 2.0 A and 1.8 A resolution, respectively. The structure of the GPb-Acurea complex reveals that the inhibitor can be accommodated in the catalytic site of T-state GPb with very little change in the tertiary structure. The glucopyranose moiety makes the standard hydrogen bonds and van der Waals contacts as observed in the GPb-glucose complex, while the acetyl urea moiety is in a favourable electrostatic environment and makes additional polar contacts with the protein. The structure of the GPb-Bzurea complex shows that Bzurea binds tightly at the catalytic site and induces substantial conformational changes in the vicinity of the catalytic site. In particular, the loop of the polypeptide chain containing residues 282-287 shifts 1.3-3.7 A (Calpha atoms) to accommodate Bzurea. Bzurea can also occupy the new allosteric site, some 33 A from the catalytic site, which is currently the target for the design of antidiabetic drugs.	+
-		+
-	Binding of N-acetyl-N '-beta-D-glucopyranosyl urea and N-benzoyl-N '-beta-D-glucopyranosyl urea to glycogen phosphorylase b: kinetic and crystallographic studies.,Oikonomakos NG, Kosmopoulou M, Zographos SE, Leonidas DD, Chrysina ED, Somsak L, Nagy V, Praly JP, Docsa T, Toth B, Gergely P Eur J Biochem. 2002 Mar;269(6):1684-96. PMID:11895439<ref>PMID:11895439</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3zcq" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Glycogen phosphorylase 3D structures\|Glycogen phosphorylase 3D structures]]		*[[Glycogen phosphorylase 3D structures\|Glycogen phosphorylase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
-	~~[[Category: Phosphorylase]]~~	+	[[Category: Alexacou KM]]
-	[[Category: Alexacou~~, K M~~]]	+	[[Category: Chrysina ED]]
-	[[Category: Chrysina~~, E D~~]]	+	[[Category: Docsa T]]
-	[[Category: Docsa, T]]	+	[[Category: Felfoldi N]]
-	[[Category: Felfoldi, N]]	+	[[Category: Gergely P]]
-	[[Category: Gergely, P]]	+	[[Category: Hayes JM]]
-	[[Category: Hayes~~, J M~~]]	+	[[Category: Kardakaris R]]
-	[[Category: Kardakaris, R]]	+	[[Category: Konstantakaki M]]
-	[[Category: Konstantakaki, M]]	+	[[Category: Konya B]]
-	[[Category: Konya, B]]	+	[[Category: Leonidas DD]]
-	[[Category: Leonidas~~, D D~~]]	+	[[Category: Nagy V]]
-	[[Category: Nagy, V]]	+	[[Category: Oikonomakos NG]]
-	[[Category: Oikonomakos~~, N G~~]]	+	[[Category: Praly JP]]
-	[[Category: Praly~~, J P~~]]	+	[[Category: Somsak L]]
-	[[Category: Somsak, L]]	+	[[Category: Telepo K]]
-	[[Category: Telepo, K]]	+	[[Category: Zographos SE]]
-	[[Category: Zographos~~, S E]]~~	+
-	~~[[Category: Hypoglycaemic agent]]~~	+
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Structure-based ligand design]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 05:42, 10 August 2022

OCA — Wed, 10 Aug 2022 05:42:00 GMT

←Older revision		Revision as of 05:42, 10 August 2022
Line 1:		Line 1:

	==Rabbit muscle glycogen phosphorylase b in complex with N-(4- trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution==		==Rabbit muscle glycogen phosphorylase b in complex with N-(4- trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution==
-	<StructureSection load='3zcq' size='340' side='right' caption='[[3zcq]], [[Resolution\|resolution]] 2.15Å' scene=''>	+	<StructureSection load='3zcq' size='340' side='right'caption='[[3zcq]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3zcq]] 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=3ZCQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3ZCQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3zcq]] 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=3ZCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZCQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=62N:N-{[4-(TRIFLUOROMETHYL)BENZOYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>62N</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=62N:N-{[4-(TRIFLUOROMETHYL)BENZOYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>62N</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zcp\|3zcp]], [[3zcr\|3zcr]], [[3zcs\|3zcs]], [[3zct\|3zct]], [[3zcu\|3zcu]], [[3zcv\|3zcv]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zcp\|3zcp]], [[3zcr\|3zcr]], [[3zcs\|3zcs]], [[3zct\|3zct]], [[3zcu\|3zcu]], [[3zcv\|3zcv]]</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=3zcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zcq OCA], [~~http~~://pdbe.org/3zcq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3zcq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3zcq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3zcq 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=3zcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zcq OCA], [https://pdbe.org/3zcq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zcq RCSB], [https://www.ebi.ac.uk/pdbsum/3zcq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zcq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 22:

	==See Also==		==See Also==
-	*[[Glycogen ~~Phosphorylase~~\|Glycogen ~~Phosphorylase~~]]	+	*[[Glycogen phosphorylase 3D structures\|Glycogen phosphorylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]

OCA at 16:53, 4 August 2016

OCA — Thu, 04 Aug 2016 16:53:16 GMT

←Older revision		Revision as of 16:53, 4 August 2016
Line 1:		Line 1:
		+
	==Rabbit muscle glycogen phosphorylase b in complex with N-(4- trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution==		==Rabbit muscle glycogen phosphorylase b in complex with N-(4- trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution==
	<StructureSection load='3zcq' size='340' side='right' caption='[[3zcq]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='3zcq' size='340' side='right' caption='[[3zcq]], [[Resolution\|resolution]] 2.15Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zcp\|3zcp]], [[3zcr\|3zcr]], [[3zcs\|3zcs]], [[3zct\|3zct]], [[3zcu\|3zcu]], [[3zcv\|3zcv]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zcp\|3zcp]], [[3zcr\|3zcr]], [[3zcs\|3zcs]], [[3zct\|3zct]], [[3zcu\|3zcu]], [[3zcv\|3zcv]]</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=3zcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zcq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zcq RCSB], [http://www.ebi.ac.uk/pdbsum/3zcq 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=3zcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zcq OCA], [http://pdbe.org/3zcq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zcq RCSB], [http://www.ebi.ac.uk/pdbsum/3zcq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zcq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3zcq" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 11:08, 25 December 2014

OCA — Thu, 25 Dec 2014 11:08:07 GMT

←Older revision		Revision as of 11:08, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3zcq\| PDB=3zcq \| SCENE= }}~~	+	==Rabbit muscle glycogen phosphorylase b in complex with N-(4- trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution==
-	===Rabbit muscle glycogen phosphorylase b in complex with N-(4- trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution===	+	<StructureSection load='3zcq' size='340' side='right' caption='[[3zcq]], [[Resolution\|resolution]] 2.15Å' scene=''>
-	{~~{ABSTRACT_PUBMED_11895439}~~}	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3zcq]] 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=3ZCQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZCQ FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=62N:N-{[4-(TRIFLUOROMETHYL)BENZOYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>62N</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zcp\|3zcp]], [[3zcr\|3zcr]], [[3zcs\|3zcs]], [[3zct\|3zct]], [[3zcu\|3zcu]], [[3zcv\|3zcv]]</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=3zcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zcq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zcq RCSB], [http://www.ebi.ac.uk/pdbsum/3zcq PDBsum]</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.		[[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.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Two substituted ureas of beta-D-glucose, N-acetyl-N'-beta-D-glucopyranosyl urea (Acurea) and N-benzoyl-N'-beta-D-glucopyranosyl urea (Bzurea), have been identified as inhibitors of glycogen phosphorylase, a potential target for therapeutic intervention in type 2 diabetes. To elucidate the structural basis of inhibition, we determined the structure of muscle glycogen phosphorylase b (GPb) complexed with the two compounds at 2.0 A and 1.8 A resolution, respectively. The structure of the GPb-Acurea complex reveals that the inhibitor can be accommodated in the catalytic site of T-state GPb with very little change in the tertiary structure. The glucopyranose moiety makes the standard hydrogen bonds and van der Waals contacts as observed in the GPb-glucose complex, while the acetyl urea moiety is in a favourable electrostatic environment and makes additional polar contacts with the protein. The structure of the GPb-Bzurea complex shows that Bzurea binds tightly at the catalytic site and induces substantial conformational changes in the vicinity of the catalytic site. In particular, the loop of the polypeptide chain containing residues 282-287 shifts 1.3-3.7 A (Calpha atoms) to accommodate Bzurea. Bzurea can also occupy the new allosteric site, some 33 A from the catalytic site, which is currently the target for the design of antidiabetic drugs.
		+
		+	Binding of N-acetyl-N '-beta-D-glucopyranosyl urea and N-benzoyl-N '-beta-D-glucopyranosyl urea to glycogen phosphorylase b: kinetic and crystallographic studies.,Oikonomakos NG, Kosmopoulou M, Zographos SE, Leonidas DD, Chrysina ED, Somsak L, Nagy V, Praly JP, Docsa T, Toth B, Gergely P Eur J Biochem. 2002 Mar;269(6):1684-96. PMID:11895439<ref>PMID:11895439</ref>

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3zcq]] 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=3ZCQ OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:011895439</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]
-	[[Category: Alexacou, K M.]]	+	[[Category: Alexacou, K M]]
-	[[Category: Chrysina, E D.]]	+	[[Category: Chrysina, E D]]
-	[[Category: Docsa, T.]]	+	[[Category: Docsa, T]]
-	[[Category: Felfoldi, N.]]	+	[[Category: Felfoldi, N]]
-	[[Category: Gergely, P.]]	+	[[Category: Gergely, P]]
-	[[Category: Hayes, J M.]]	+	[[Category: Hayes, J M]]
-	[[Category: Kardakaris, R.]]	+	[[Category: Kardakaris, R]]
-	[[Category: Konstantakaki, M.]]	+	[[Category: Konstantakaki, M]]
-	[[Category: Konya, B.]]	+	[[Category: Konya, B]]
-	[[Category: Leonidas, D D.]]	+	[[Category: Leonidas, D D]]
-	[[Category: Nagy, V.]]	+	[[Category: Nagy, V]]
-	[[Category: Oikonomakos, N G.]]	+	[[Category: Oikonomakos, N G]]
-	[[Category: Praly, J P.]]	+	[[Category: Praly, J P]]
-	[[Category: Somsak, L.]]	+	[[Category: Somsak, L]]
-	[[Category: Telepo, K.]]	+	[[Category: Telepo, K]]
-	[[Category: Zographos, S E.]]	+	[[Category: Zographos, S E]]
	[[Category: Hypoglycaemic agent]]		[[Category: Hypoglycaemic agent]]
	[[Category: Inhibitor]]		[[Category: Inhibitor]]
	[[Category: Structure-based ligand design]]		[[Category: Structure-based ligand design]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 13:33, 11 December 2013

OCA — Wed, 11 Dec 2013 13:33:17 GMT

←Older revision		Revision as of 13:33, 11 December 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_3zcq\| PDB=3zcq \| SCENE= }}
		+	===Rabbit muscle glycogen phosphorylase b in complex with N-(4- trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution===
		+	{{ABSTRACT_PUBMED_11895439}}

-	~~The entry 3zcq~~ is ~~ON HOLD until Paper Publication~~	+	==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.

-	~~Authors~~: ~~Chrysina, E~~.D.~~, Nagy, V~~.~~, Felfoldi, N., Konya, B., Telepo, K., Praly, J.P., Docsa, T., Gergely, P., Alexacou, K.M., Hayes, J.M., Konstantakaki, M., Kardakaris, R., Leonidas, D.D., Zographos, S.E~~.~~, Oikonomakos, N~~.G.~~, Somsak, L~~.	+	==About this Structure==
		+	[[3zcq]] 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=3ZCQ OCA].

-	~~Description~~: ~~Rabbit muscle glycogen phosphorylase b in complex with~~ N~~-(4-trifluoromethyl-benzoyl)-N-beta-~~D~~-glucopyranosyl urea determined at 2~~. ~~15 A resolution~~	+	==Reference==
		+	<ref group="xtra">PMID:011895439</ref><references group="xtra"/><references/>
		+	[[Category: Oryctolagus cuniculus]]
		+	[[Category: Phosphorylase]]
		+	[[Category: Alexacou, K M.]]
		+	[[Category: Chrysina, E D.]]
		+	[[Category: Docsa, T.]]
		+	[[Category: Felfoldi, N.]]
		+	[[Category: Gergely, P.]]
		+	[[Category: Hayes, J M.]]
		+	[[Category: Kardakaris, R.]]
		+	[[Category: Konstantakaki, M.]]
		+	[[Category: Konya, B.]]
		+	[[Category: Leonidas, D D.]]
		+	[[Category: Nagy, V.]]
		+	[[Category: Oikonomakos, N G.]]
		+	[[Category: Praly, J P.]]
		+	[[Category: Somsak, L.]]
		+	[[Category: Telepo, K.]]
		+	[[Category: Zographos, S E.]]
		+	[[Category: Hypoglycaemic agent]]
		+	[[Category: Inhibitor]]
		+	[[Category: Structure-based ligand design]]
		+	[[Category: Transferase]]

OCA at 10:18, 5 December 2012

OCA — Wed, 05 Dec 2012 10:18:32 GMT

←Older revision		Revision as of 10:18, 5 December 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3zcq is ON HOLD	+	The entry 3zcq is ON HOLD until Paper Publication

	Authors: Chrysina, E.D., Nagy, V., Felfoldi, N., Konya, B., Telepo, K., Praly, J.P., Docsa, T., Gergely, P., Alexacou, K.M., Hayes, J.M., Konstantakaki, M., Kardakaris, R., Leonidas, D.D., Zographos, S.E., Oikonomakos, N.G., Somsak, L.		Authors: Chrysina, E.D., Nagy, V., Felfoldi, N., Konya, B., Telepo, K., Praly, J.P., Docsa, T., Gergely, P., Alexacou, K.M., Hayes, J.M., Konstantakaki, M., Kardakaris, R., Leonidas, D.D., Zographos, S.E., Oikonomakos, N.G., Somsak, L.

	Description: Rabbit muscle glycogen phosphorylase b in complex with N-(4-trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution		Description: Rabbit muscle glycogen phosphorylase b in complex with N-(4-trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution

OCA: Protected "3zcq" [edit=sysop:move=sysop]

OCA — Wed, 28 Nov 2012 13:52:00 GMT

Protected "3zcq" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:52, 28 November 2012

OCA: New page: '''Unreleased structure''' The entry 3zcq is ON HOLD Authors: Chrysina, E.D., Nagy, V., Felfoldi, N., Konya, B., Telepo, K., Praly, J.P., Docsa, T., Gergely, P., Alexacou, K.M., Hayes, ...

OCA — Wed, 28 Nov 2012 13:51:59 GMT

New page: '''Unreleased structure''' The entry 3zcq is ON HOLD Authors: Chrysina, E.D., Nagy, V., Felfoldi, N., Konya, B., Telepo, K., Praly, J.P., Docsa, T., Gergely, P., Alexacou, K.M., Hayes, ...

New page

'''Unreleased structure'''

The entry 3zcq is ON HOLD

Authors: Chrysina, E.D., Nagy, V., Felfoldi, N., Konya, B., Telepo, K., Praly, J.P., Docsa, T., Gergely, P., Alexacou, K.M., Hayes, J.M., Konstantakaki, M., Kardakaris, R., Leonidas, D.D., Zographos, S.E., Oikonomakos, N.G., Somsak, L.

Description: Rabbit muscle glycogen phosphorylase b in complex with N-(4-trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution