4laz - Revision history

OCA at 16:15, 20 September 2023

OCA — Wed, 20 Sep 2023 16:15:44 GMT

←Older revision		Revision as of 16:15, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4laz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LAZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4laz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LAZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1WW:{5-CHLORO-2-[(4-IODOBENZYL)CARBAMOYL]PHENOXY}ACETIC+ACID'>1WW</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 0.85Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1WW:{5-CHLORO-2-[(4-IODOBENZYL)CARBAMOYL]PHENOXY}ACETIC+ACID'>1WW</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=4laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4laz OCA], [https://pdbe.org/4laz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4laz RCSB], [https://www.ebi.ac.uk/pdbsum/4laz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4laz 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=4laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4laz OCA], [https://pdbe.org/4laz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4laz RCSB], [https://www.ebi.ac.uk/pdbsum/4laz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4laz ProSAT]</span></td></tr>
	</table>		</table>

OCA at 10:49, 14 December 2022

OCA — Wed, 14 Dec 2022 10:49:06 GMT

←Older revision		Revision as of 10:49, 14 December 2022
Line 1:		Line 1:

	==Crystal structure of human AR complexed with NADP+ and {5-chloro-2-[(4-iodobenzyl)carbamoyl]phenoxy}acetic acid==		==Crystal structure of human AR complexed with NADP+ and {5-chloro-2-[(4-iodobenzyl)carbamoyl]phenoxy}acetic acid==
-	<StructureSection load='4laz' size='340' side='right' caption='[[4laz]], [[Resolution\|resolution]] 0.85Å' scene=''>	+	<StructureSection load='4laz' size='340' side='right'caption='[[4laz]], [[Resolution\|resolution]] 0.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4laz]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4LAZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4laz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LAZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1WW:{5-CHLORO-2-[(4-IODOBENZYL)CARBAMOYL]PHENOXY}ACETIC+ACID'>1WW</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1WW:{5-CHLORO-2-[(4-IODOBENZYL)CARBAMOYL]PHENOXY}ACETIC+ACID'>1WW</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1us0\|1us0]], [[2iki\|2iki]], [[4lau\|4lau]], [[4lb3\|4lb3]], [[4lb4\|4lb4]], [[4lbr\|4lbr]], [[4lbs\|4lbs]]</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=4laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4laz OCA], [https://pdbe.org/4laz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4laz RCSB], [https://www.ebi.ac.uk/pdbsum/4laz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4laz ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AKR1B1, ALDR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </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=4laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4laz OCA], [~~http~~://pdbe.org/4laz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4laz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4laz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4laz ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN]] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.	+	[https://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4laz" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4laz" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aldose reductase 3D structures\|Aldose reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Aldehyde reductase~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Cousido-Siah, A]]	+	[[Category: Cousido-Siah A]]
-	[[Category: Fanfrlik, J]]	+	[[Category: Fanfrlik J]]
-	[[Category: Hobza, P]]	+	[[Category: Hobza P]]
-	[[Category: Kolar, M]]	+	[[Category: Kolar M]]
-	[[Category: Mitschler, A]]	+	[[Category: Mitschler A]]
-	[[Category: Podjarny, A]]	+	[[Category: Podjarny A]]
-	[[Category: Ruiz~~, F X]]~~	+	[[Category: Ruiz FX]]
-	~~[[Category: Aldose reductase]]~~	+
-	~~[[Category: Cytosolic]]~~	+
-	~~[[Category: Diabetes]]~~	+
-	~~[[Category: Halogenated compound]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Tim barrel~~]]	+

OCA at 09:35, 15 November 2017

OCA — Wed, 15 Nov 2017 09:35:30 GMT

←Older revision		Revision as of 09:35, 15 November 2017
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4laz" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4laz" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Aldose Reductase\|Aldose Reductase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 05:15, 5 August 2016

OCA — Fri, 05 Aug 2016 05:15:59 GMT

←Older revision		Revision as of 05:15, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of human AR complexed with NADP+ and {5-chloro-2-[(4-iodobenzyl)carbamoyl]phenoxy}acetic acid==		==Crystal structure of human AR complexed with NADP+ and {5-chloro-2-[(4-iodobenzyl)carbamoyl]phenoxy}acetic acid==
	<StructureSection load='4laz' size='340' side='right' caption='[[4laz]], [[Resolution\|resolution]] 0.85Å' scene=''>		<StructureSection load='4laz' size='340' side='right' caption='[[4laz]], [[Resolution\|resolution]] 0.85Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AKR1B1, ALDR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AKR1B1, ALDR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </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=4laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4laz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4laz RCSB], [http://www.ebi.ac.uk/pdbsum/4laz 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=4laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4laz OCA], [http://pdbe.org/4laz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4laz RCSB], [http://www.ebi.ac.uk/pdbsum/4laz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4laz 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 4laz" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aldose Reductase\|Aldose Reductase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 23:17, 24 December 2014

OCA — Wed, 24 Dec 2014 23:17:45 GMT

←Older revision		Revision as of 23:17, 24 December 2014
Line 2:		Line 2:
	<StructureSection load='4laz' size='340' side='right' caption='[[4laz]], [[Resolution\|resolution]] 0.85Å' scene=''>		<StructureSection load='4laz' size='340' side='right' caption='[[4laz]], [[Resolution\|resolution]] 0.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4laz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAZ OCA]. <br>	+	<table><tr><td colspan='2'>[[4laz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LAZ FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1WW:{5-CHLORO-2-[(4-IODOBENZYL)CARBAMOYL]PHENOXY}ACETIC+ACID'>1WW</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1WW:{5-CHLORO-2-[(4-IODOBENZYL)CARBAMOYL]PHENOXY}ACETIC+ACID'>1WW</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1us0\|1us0]], [[2iki\|2iki]], [[4lau\|4lau]], [[4lb3\|4lb3]], [[4lb4\|4lb4]], [[4lbr\|4lbr]], [[4lbs\|4lbs]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1us0\|1us0]], [[2iki\|2iki]], [[4lau\|4lau]], [[4lb3\|4lb3]], [[4lb4\|4lb4]], [[4lbr\|4lbr]], [[4lbs\|4lbs]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Glucokinase Glucokinase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.~~2 2~~.7.1.2] </span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AKR1B1, ALDR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4laz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4laz RCSB], [http://www.ebi.ac.uk/pdbsum/4laz PDBsum]</span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </span></td></tr>
-	<table>	+	<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=4laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4laz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4laz RCSB], [http://www.ebi.ac.uk/pdbsum/4laz PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN]] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 17:
	Modulation of aldose reductase inhibition by halogen bond tuning.,Fanfrlik J, Kolar M, Kamlar M, Hurny D, Ruiz FX, Cousido-Siah A, Mitschler A, Rezac J, Munusamy E, Lepsik M, Matejicek P, Vesely J, Podjarny A, Hobza P ACS Chem Biol. 2013 Nov 15;8(11):2484-92. doi: 10.1021/cb400526n. Epub 2013 Sep, 17. PMID:23988122<ref>PMID:23988122</ref>		Modulation of aldose reductase inhibition by halogen bond tuning.,Fanfrlik J, Kolar M, Kamlar M, Hurny D, Ruiz FX, Cousido-Siah A, Mitschler A, Rezac J, Munusamy E, Lepsik M, Matejicek P, Vesely J, Podjarny A, Hobza P ACS Chem Biol. 2013 Nov 15;8(11):2484-92. doi: 10.1021/cb400526n. Epub 2013 Sep, 17. PMID:23988122<ref>PMID:23988122</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 21:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Aldehyde reductase]]		[[Category: Aldehyde reductase]]
-	[[Category: Cousido-Siah, A.]]	+	[[Category: Human]]
-	[[Category: Fanfrlik, J.]]	+	[[Category: Cousido-Siah, A]]
-	[[Category: Hobza, P.]]	+	[[Category: Fanfrlik, J]]
-	[[Category: Kolar, M.]]	+	[[Category: Hobza, P]]
-	[[Category: Mitschler, A.]]	+	[[Category: Kolar, M]]
-	[[Category: Podjarny, A.]]	+	[[Category: Mitschler, A]]
-	[[Category: Ruiz, F X.]]	+	[[Category: Podjarny, A]]
		+	[[Category: Ruiz, F X]]
	[[Category: Aldose reductase]]		[[Category: Aldose reductase]]
	[[Category: Cytosolic]]		[[Category: Cytosolic]]

OCA at 09:27, 1 May 2014

OCA — Thu, 01 May 2014 09:27:34 GMT

←Older revision		Revision as of 09:27, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='4laz' size='340' side='right' caption='[[4laz]], [[Resolution\|resolution]] 0.85Å' scene=''>		<StructureSection load='4laz' size='340' side='right' caption='[[4laz]], [[Resolution\|resolution]] 0.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	[[4laz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAZ OCA]. <br>	+	<table><tr><td colspan='2'>[[4laz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAZ OCA]. <br>
-	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=1WW:{5-CHLORO-2-[(4-IODOBENZYL)CARBAMOYL]PHENOXY}ACETIC+ACID'>1WW</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene><br>	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1WW:{5-CHLORO-2-[(4-IODOBENZYL)CARBAMOYL]PHENOXY}ACETIC+ACID'>1WW</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene><br>
-	<b>[[Related_structure\|Related:]]</b> [[1us0\|1us0]], [[2iki\|2iki]], [[4lau\|4lau]], [[4lb3\|4lb3]], [[4lb4\|4lb4]], [[4lbr\|4lbr]], [[4lbs\|4lbs]]<br>	+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1us0\|1us0]], [[2iki\|2iki]], [[4lau\|4lau]], [[4lb3\|4lb3]], [[4lb4\|4lb4]], [[4lbr\|4lbr]], [[4lbs\|4lbs]]</td></tr>
-	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
-	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4laz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4laz RCSB], [http://www.ebi.ac.uk/pdbsum/4laz PDBsum]</span><br>	+	<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=4laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4laz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4laz RCSB], [http://www.ebi.ac.uk/pdbsum/4laz PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	In this paper, we studied a designed series of aldose reductase (AR) inhibitors. The series was derived from a known AR binder, which had previously been shown to form a halogen bond between its bromine atom and the oxygen atom of the Thr-113 side chain of AR. In the series, the strength of the halogen bond was modulated by two factors, namely bromine-iodine substitution and the fluorination of the aromatic ring in several positions. The role of the single halogen bond in AR-ligand binding was elucidated by advanced binding free energy calculations involving the semiempirical quantum chemical Hamiltonian. The results were complemented with ultrahigh-resolution X-ray crystallography and IC50 measurements. All of the AR inhibitors studied were shown by X-ray crystallography to bind in an identical manner. Further, it was demonstrated that it was possible to decrease the IC50 value by about 1 order of magnitude by tuning the strength of the halogen bond by a monoatomic substitution. The calculations revealed that the protein-ligand interaction energy increased upon the substitution of iodine for bromine or upon the addition of electron-withdrawing fluorine atoms to the ring. However, the effect on the binding affinity was found to be more complex due to the change of the solvation/desolvation properties within the ligand series. The study shows that it is possible to modulate the strength of a halogen bond in a protein-ligand complex as was designed based on the previous studies of low-molecular-weight complexes.		In this paper, we studied a designed series of aldose reductase (AR) inhibitors. The series was derived from a known AR binder, which had previously been shown to form a halogen bond between its bromine atom and the oxygen atom of the Thr-113 side chain of AR. In the series, the strength of the halogen bond was modulated by two factors, namely bromine-iodine substitution and the fluorination of the aromatic ring in several positions. The role of the single halogen bond in AR-ligand binding was elucidated by advanced binding free energy calculations involving the semiempirical quantum chemical Hamiltonian. The results were complemented with ultrahigh-resolution X-ray crystallography and IC50 measurements. All of the AR inhibitors studied were shown by X-ray crystallography to bind in an identical manner. Further, it was demonstrated that it was possible to decrease the IC50 value by about 1 order of magnitude by tuning the strength of the halogen bond by a monoatomic substitution. The calculations revealed that the protein-ligand interaction energy increased upon the substitution of iodine for bromine or upon the addition of electron-withdrawing fluorine atoms to the ring. However, the effect on the binding affinity was found to be more complex due to the change of the solvation/desolvation properties within the ligand series. The study shows that it is possible to modulate the strength of a halogen bond in a protein-ligand complex as was designed based on the previous studies of low-molecular-weight complexes.
Line 13:		Line 15:

	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:58, 30 April 2014

OCA — Wed, 30 Apr 2014 09:58:41 GMT

←Older revision		Revision as of 09:58, 30 April 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	[[4laz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAZ OCA]. <br>		[[4laz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAZ OCA]. <br>
-	<b>Related:</b> [[1us0\|1us0]], [[2iki\|2iki]], [[4lau\|4lau]], [[4lb3\|4lb3]], [[4lb4\|4lb4]], [[4lbr\|4lbr]], [[4lbs\|4lbs]]<br>	+	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=1WW:{5-CHLORO-2-[(4-IODOBENZYL)CARBAMOYL]PHENOXY}ACETIC+ACID'>1WW</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene><br>
		+	<b>[[Related_structure\|Related:]]</b> [[1us0\|1us0]], [[2iki\|2iki]], [[4lau\|4lau]], [[4lb3\|4lb3]], [[4lb4\|4lb4]], [[4lbr\|4lbr]], [[4lbs\|4lbs]]<br>
	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>		<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4laz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4laz RCSB], [http://www.ebi.ac.uk/pdbsum/4laz PDBsum]</span><br>
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	In this paper, we studied a designed series of aldose reductase (AR) inhibitors. The series was derived from a known AR binder, which had previously been shown to form a halogen bond between its bromine atom and the oxygen atom of the Thr-113 side chain of AR. In the series, the strength of the halogen bond was modulated by two factors, namely bromine-iodine substitution and the fluorination of the aromatic ring in several positions. The role of the single halogen bond in AR-ligand binding was elucidated by advanced binding free energy calculations involving the semiempirical quantum chemical Hamiltonian. The results were complemented with ultrahigh-resolution X-ray crystallography and IC50 measurements. All of the AR inhibitors studied were shown by X-ray crystallography to bind in an identical manner. Further, it was demonstrated that it was possible to decrease the IC50 value by about 1 order of magnitude by tuning the strength of the halogen bond by a monoatomic substitution. The calculations revealed that the protein-ligand interaction energy increased upon the substitution of iodine for bromine or upon the addition of electron-withdrawing fluorine atoms to the ring. However, the effect on the binding affinity was found to be more complex due to the change of the solvation/desolvation properties within the ligand series. The study shows that it is possible to modulate the strength of a halogen bond in a protein-ligand complex as was designed based on the previous studies of low-molecular-weight complexes.		In this paper, we studied a designed series of aldose reductase (AR) inhibitors. The series was derived from a known AR binder, which had previously been shown to form a halogen bond between its bromine atom and the oxygen atom of the Thr-113 side chain of AR. In the series, the strength of the halogen bond was modulated by two factors, namely bromine-iodine substitution and the fluorination of the aromatic ring in several positions. The role of the single halogen bond in AR-ligand binding was elucidated by advanced binding free energy calculations involving the semiempirical quantum chemical Hamiltonian. The results were complemented with ultrahigh-resolution X-ray crystallography and IC50 measurements. All of the AR inhibitors studied were shown by X-ray crystallography to bind in an identical manner. Further, it was demonstrated that it was possible to decrease the IC50 value by about 1 order of magnitude by tuning the strength of the halogen bond by a monoatomic substitution. The calculations revealed that the protein-ligand interaction energy increased upon the substitution of iodine for bromine or upon the addition of electron-withdrawing fluorine atoms to the ring. However, the effect on the binding affinity was found to be more complex due to the change of the solvation/desolvation properties within the ligand series. The study shows that it is possible to modulate the strength of a halogen bond in a protein-ligand complex as was designed based on the previous studies of low-molecular-weight complexes.

OCA at 07:41, 30 April 2014

OCA — Wed, 30 Apr 2014 07:41:35 GMT

←Older revision		Revision as of 07:41, 30 April 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of human AR complexed with NADP+ and {5-chloro-2-[(4-iodobenzyl)carbamoyl]phenoxy}acetic acid==
		+	<StructureSection load='4laz' size='340' side='right' caption='[[4laz]], [[Resolution\|resolution]] 0.85Å' scene=''>
		+	== Structural highlights ==
		+	[[4laz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAZ OCA]. <br>
		+	<b>Related:</b> [[1us0\|1us0]], [[2iki\|2iki]], [[4lau\|4lau]], [[4lb3\|4lb3]], [[4lb4\|4lb4]], [[4lbr\|4lbr]], [[4lbs\|4lbs]]<br>
		+	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	== Publication Abstract from PubMed ==
		+	In this paper, we studied a designed series of aldose reductase (AR) inhibitors. The series was derived from a known AR binder, which had previously been shown to form a halogen bond between its bromine atom and the oxygen atom of the Thr-113 side chain of AR. In the series, the strength of the halogen bond was modulated by two factors, namely bromine-iodine substitution and the fluorination of the aromatic ring in several positions. The role of the single halogen bond in AR-ligand binding was elucidated by advanced binding free energy calculations involving the semiempirical quantum chemical Hamiltonian. The results were complemented with ultrahigh-resolution X-ray crystallography and IC50 measurements. All of the AR inhibitors studied were shown by X-ray crystallography to bind in an identical manner. Further, it was demonstrated that it was possible to decrease the IC50 value by about 1 order of magnitude by tuning the strength of the halogen bond by a monoatomic substitution. The calculations revealed that the protein-ligand interaction energy increased upon the substitution of iodine for bromine or upon the addition of electron-withdrawing fluorine atoms to the ring. However, the effect on the binding affinity was found to be more complex due to the change of the solvation/desolvation properties within the ligand series. The study shows that it is possible to modulate the strength of a halogen bond in a protein-ligand complex as was designed based on the previous studies of low-molecular-weight complexes.

-	~~The entry 4laz is ON HOLD until Paper Publication~~	+	Modulation of aldose reductase inhibition by halogen bond tuning.,Fanfrlik J, Kolar M, Kamlar M, Hurny D, Ruiz FX, Cousido-Siah A, Mitschler A, Rezac J, Munusamy E, Lepsik M, Matejicek P, Vesely J, Podjarny A, Hobza P ACS Chem Biol. 2013 Nov 15;8(11):2484-92. doi: 10.1021/cb400526n. Epub 2013 Sep, 17. PMID:23988122<ref>PMID:23988122</ref>

-	~~Authors~~: Cousido-Siah, A.~~, Mitschler, A., Ruiz, F.X.,~~ Fanfrlik, J., Kolar, M., ~~Hobza, P~~., Podjarny, A.	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	== References ==
-	~~Description~~: ~~Crystal structure of human AR complexed with NADP+ and {5-chloro-2-~~[~~(4-iodobenzyl)carbamoyl~~]~~phenoxy}acetic acid~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Aldehyde reductase]]
		+	[[Category: Cousido-Siah, A.]]
		+	[[Category: Fanfrlik, J.]]
		+	[[Category: Hobza, P.]]
		+	[[Category: Kolar, M.]]
		+	[[Category: Mitschler, A.]]
		+	[[Category: Podjarny, A.]]
		+	[[Category: Ruiz, F X.]]
		+	[[Category: Aldose reductase]]
		+	[[Category: Cytosolic]]
		+	[[Category: Diabetes]]
		+	[[Category: Halogenated compound]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Tim barrel]]

OCA at 12:25, 24 July 2013

OCA — Wed, 24 Jul 2013 12:25:55 GMT

←Older revision		Revision as of 12:25, 24 July 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4laz is ON HOLD	+	The entry 4laz is ON HOLD until Paper Publication

	Authors: Cousido-Siah, A., Mitschler, A., Ruiz, F.X., Fanfrlik, J., Kolar, M., Hobza, P., Podjarny, A.		Authors: Cousido-Siah, A., Mitschler, A., Ruiz, F.X., Fanfrlik, J., Kolar, M., Hobza, P., Podjarny, A.

-	Description: Crystal structure of human AR complexed with NADP+ and ~~MK257~~	+	Description: Crystal structure of human AR complexed with NADP+ and {5-chloro-2-[(4-iodobenzyl)carbamoyl]phenoxy}acetic acid

OCA: Protected "4laz" [edit=sysop:move=sysop]

OCA — Sun, 30 Jun 2013 09:12:03 GMT

Protected "4laz" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:12, 30 June 2013