4ej2 - Revision history

OCA at 15:02, 14 March 2024

2024-03-14T15:02:45Z

← Older revision		Revision as of 15:02, 14 March 2024
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	== 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 ==~~
	C5-alkynyl and alkylfurano[2,3-d]pyrimidine glucopyranonucleosides have been synthesized and studied as inhibitors of glycogen phosphorylase b (GPb). Kinetic experiments have shown that most of these compounds were low micromolar inhibitors of the enzyme. The best inhibitor was 1-(beta-d-glucopyranosyl)-5-ethynyluracil (K(i)=4.7muM). Crystallographic analysis of these compounds in complex with GPb revealed that inhibitors with a long C5-alkynyl group exploited interactions with beta-pocket of the active site and induced significant conformational changes of the 280s loop compared to GPb in complex with compounds with a short C5-alkynyl group. The results highlight the importance in the length of the aliphatic groups used to enhance inhibitory potency for the exploitation of the hydrophobic beta-pocket. The best of the inhibitors had also a moderate effect on glycogenolysis in the cellular lever with an IC(50) value of 291.4muM.

	The binding of C5-alkynyl and alkylfurano[2,3-d]pyrimidine glucopyranonucleosides to glycogen phosphorylase b: Synthesis, biochemical and biological assessment.,Kantsadi AL, Manta S, Psarra AM, Dimopoulou A, Kiritsis C, Parmenopoulou V, Skamnaki VT, Zoumpoulakis P, Zographos SE, Leonidas DD, Komiotis D Eur J Med Chem. 2012 Jun 22. PMID:22770609<ref>PMID:22770609</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4ej2" 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>

OCA at 08:21, 6 December 2023

2023-12-06T08:21:38Z

← Older revision		Revision as of 08:21, 6 December 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ej2]] 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=4EJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EJ2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ej2]] 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=4EJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EJ2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D1F:1-(BETA-D-GLUCOPYRANOSYL)-5-(HEPT-1-YN-1-YL)PYRIMIDINE-2,4(1H,3H)-DIONE'>D1F</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>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.65Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D1F:1-(BETA-D-GLUCOPYRANOSYL)-5-(HEPT-1-YN-1-YL)PYRIMIDINE-2,4(1H,3H)-DIONE'>D1F</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>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ej2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ej2 OCA], [https://pdbe.org/4ej2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ej2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ej2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ej2 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=4ej2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ej2 OCA], [https://pdbe.org/4ej2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ej2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ej2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ej2 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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 07:13, 28 September 2022

2022-09-28T07:13:37Z

← Older revision		Revision as of 07:13, 28 September 2022
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	<StructureSection load='4ej2' size='340' side='right'caption='[[4ej2]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='4ej2' size='340' side='right'caption='[[4ej2]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ej2]] 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=4EJ2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4EJ2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ej2]] 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=4EJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EJ2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D1F:1-(BETA-D-GLUCOPYRANOSYL)-5-(HEPT-1-YN-1-YL)PYRIMIDINE-2,4(1H,3H)-DIONE'>D1F</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D1F:1-(BETA-D-GLUCOPYRANOSYL)-5-(HEPT-1-YN-1-YL)PYRIMIDINE-2,4(1H,3H)-DIONE'>D1F</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>
	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene~~></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=4ej2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ej2 OCA], [https://pdbe.org/4ej2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ej2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ej2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ej2 ProSAT]</span></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eke\|4eke]], [[4eky\|4eky]], [[4el0\|4el0]], [[4el5\|4el5]]</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=4ej2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ej2 OCA], [~~http~~://pdbe.org/4ej2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ej2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ej2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ej2 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 ==
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	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	~~[[Category: Phosphorylase]]~~		[[Category: Kantsadi AL]]
	[[Category: Kantsadi~~, A L~~]]		[[Category: Leonidas DD]]
	[[Category: Leonidas~~, D D~~]]		[[Category: Skamnaki VT]]
	[[Category: Skamnaki~~, V T]]~~
	~~[[Category: Alpha/beta protein]]~~
	~~[[Category: Transferase~~]]

OCA at 09:48, 5 February 2020

2020-02-05T09:48:51Z

← Older revision		Revision as of 09:48, 5 February 2020
Line 1:		Line 1:

	==Crystal structure of GPb in complex with DK10==		==Crystal structure of GPb in complex with DK10==
	<StructureSection load='4ej2' size='340' side='right' caption='[[4ej2]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='4ej2' size='340' side='right'caption='[[4ej2]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ej2]] 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=4EJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EJ2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ej2]] 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=4EJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EJ2 FirstGlance]. <br>
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4ej2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4ej2" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[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 08:04, 15 November 2017

2017-11-15T08:04:59Z

← Older revision		Revision as of 08:04, 15 November 2017
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4ej2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4ej2" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:15, 4 August 2016

2016-08-04T15:15:42Z

← Older revision		Revision as of 15:15, 4 August 2016
Line 1:		Line 1:

	==Crystal structure of GPb in complex with DK10==		==Crystal structure of GPb in complex with DK10==
	<StructureSection load='4ej2' size='340' side='right' caption='[[4ej2]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='4ej2' size='340' side='right' caption='[[4ej2]], [[Resolution\|resolution]] 2.65Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4ej2]] 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=4EJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EJ2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ej2]] 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=4EJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EJ2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D1F:1-(BETA-D-GLUCOPYRANOSYL)-5-(HEPT-1-YN-1-YL)PYRIMIDINE-2,4(1H,3H)-DIONE'>D1F</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D1F:1-(BETA-D-GLUCOPYRANOSYL)-5-(HEPT-1-YN-1-YL)PYRIMIDINE-2,4(1H,3H)-DIONE'>D1F</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-~~LYSINE(~~3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-~~YLMETHANE)~~'>LLP</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eke\|4eke]], [[4eky\|4eky]], [[4el0\|4el0]], [[4el5\|4el5]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eke\|4eke]], [[4eky\|4eky]], [[4el0\|4el0]], [[4el5\|4el5]]</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=4ej2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ej2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ej2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ej2 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=4ej2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ej2 OCA], [http://pdbe.org/4ej2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ej2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ej2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ej2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4ej2" style="background-color:#fffaf0;"></div>

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

OCA at 16:16, 24 December 2014

2014-12-24T16:16:33Z

← Older revision		Revision as of 16:16, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ej2]] 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=4EJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EJ2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ej2]] 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=4EJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EJ2 FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D1F:1-(BETA-D-GLUCOPYRANOSYL)-5-(HEPT-1-YN-1-YL)PYRIMIDINE-2,4(1H,3H)-DIONE'>D1F</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D1F:1-(BETA-D-GLUCOPYRANOSYL)-5-(HEPT-1-YN-1-YL)PYRIMIDINE-2,4(1H,3H)-DIONE'>D1F</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eke\|4eke]], [[4eky\|4eky]], [[4el0\|4el0]], [[4el5\|4el5]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eke\|4eke]], [[4eky\|4eky]], [[4el0\|4el0]], [[4el5\|4el5]]</td></tr>
	<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>		<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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ej2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ej2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ej2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ej2 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=4ej2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ej2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ej2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ej2 PDBsum]</span></td></tr>
	<table>		</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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 28:
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]
	[[Category: Kantsadi, A L.]]		[[Category: Kantsadi, A L]]
	[[Category: Leonidas, D D.]]		[[Category: Leonidas, D D]]
	[[Category: Skamnaki, V T.]]		[[Category: Skamnaki, V T]]
	[[Category: Alpha/beta protein]]		[[Category: Alpha/beta protein]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 09:14, 11 June 2014

2014-06-11T09:14:55Z

← Older revision		Revision as of 09:14, 11 June 2014
Line 1:		Line 1:
	[[~~Image~~:~~4ej2~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of GPb in complex with DK10==
			<StructureSection load='4ej2' size='340' side='right' caption='[[4ej2]], [[Resolution\|resolution]] 2.65Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4ej2]] 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=4EJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EJ2 FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D1F:1-(BETA-D-GLUCOPYRANOSYL)-5-(HEPT-1-YN-1-YL)PYRIMIDINE-2,4(1H,3H)-DIONE'>D1F</scene><br>
			<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eke\|4eke]], [[4eky\|4eky]], [[4el0\|4el0]], [[4el5\|4el5]]</td></tr>
			<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>
			<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=4ej2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ej2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ej2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ej2 PDBsum]</span></td></tr>
			<table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			C5-alkynyl and alkylfurano[2,3-d]pyrimidine glucopyranonucleosides have been synthesized and studied as inhibitors of glycogen phosphorylase b (GPb). Kinetic experiments have shown that most of these compounds were low micromolar inhibitors of the enzyme. The best inhibitor was 1-(beta-d-glucopyranosyl)-5-ethynyluracil (K(i)=4.7muM). Crystallographic analysis of these compounds in complex with GPb revealed that inhibitors with a long C5-alkynyl group exploited interactions with beta-pocket of the active site and induced significant conformational changes of the 280s loop compared to GPb in complex with compounds with a short C5-alkynyl group. The results highlight the importance in the length of the aliphatic groups used to enhance inhibitory potency for the exploitation of the hydrophobic beta-pocket. The best of the inhibitors had also a moderate effect on glycogenolysis in the cellular lever with an IC(50) value of 291.4muM.

	~~{{STRUCTURE_4ej2\| PDB=4ej2 \| SCENE= }}~~		The binding of C5-alkynyl and alkylfurano[2,3-d]pyrimidine glucopyranonucleosides to glycogen phosphorylase b: Synthesis, biochemical and biological assessment.,Kantsadi AL, Manta S, Psarra AM, Dimopoulou A, Kiritsis C, Parmenopoulou V, Skamnaki VT, Zoumpoulakis P, Zographos SE, Leonidas DD, Komiotis D Eur J Med Chem. 2012 Jun 22. PMID:22770609<ref>PMID:22770609</ref>

	~~===Crystal structure~~ of ~~GPb in complex with DK10===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_22770609}}~~		==See Also==
			*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]
	==~~About this Structure~~==		== References ==
	[[~~4ej2]] 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=4EJ2 OCA~~].		<references/>
			__TOC__
	==~~Reference~~==		</StructureSection>
	<~~ref group="xtra">PMID:022770609<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]

OCA at 04:56, 15 August 2012

2012-08-15T04:56:56Z

← Older revision		Revision as of 04:56, 15 August 2012
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	[[Image:4ej2.~~jpg~~\|left\|200px]]		[[Image:4ej2.png\|left\|200px]]

	{{STRUCTURE_4ej2\| PDB=4ej2 \| SCENE= }}		{{STRUCTURE_4ej2\| PDB=4ej2 \| SCENE= }}

OCA at 07:11, 25 July 2012

2012-07-25T07:11:19Z

← Older revision		Revision as of 07:11, 25 July 2012
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	~~'''Unreleased structure'''~~		[[Image:4ej2.jpg\|left\|200px]]

	~~The entry~~ 4ej2 ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4ej2\| PDB=4ej2 \| SCENE= }}

	~~Authors: Kantsadi, A.L., Skamnaki, V.T., Leonidas, D.D.~~		===Crystal structure of GPb in complex with DK10===

	~~Description: Crystal~~ structure ~~of GPb in complex~~ with ~~DK10~~		{{ABSTRACT_PUBMED_22770609}}

			==About this Structure==
			[[4ej2]] 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=4EJ2 OCA].

			==Reference==
			<ref group="xtra">PMID:022770609</ref><references group="xtra"/>
			[[Category: Oryctolagus cuniculus]]
			[[Category: Phosphorylase]]
			[[Category: Kantsadi, A L.]]
			[[Category: Leonidas, D D.]]
			[[Category: Skamnaki, V T.]]
			[[Category: Alpha/beta protein]]
			[[Category: Transferase]]