1bu8 - Revision history

OCA at 05:42, 9 August 2023

OCA — Wed, 09 Aug 2023 05:42:39 GMT

←Older revision		Revision as of 05:42, 9 August 2023
Line 1:		Line 1:

	==RAT PANCREATIC LIPASE RELATED PROTEIN 2==		==RAT PANCREATIC LIPASE RELATED PROTEIN 2==
-	<StructureSection load='1bu8' size='340' side='right'caption='[[1bu8]]' scene=''>	+	<StructureSection load='1bu8' size='340' side='right'caption='[[1bu8]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1bu8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>
-	</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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [https://pdbe.org/1bu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [https://www.ebi.ac.uk/pdbsum/1bu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bu8 ProSAT]</span></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]] 1.8Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [https://pdbe.org/1bu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [https://www.ebi.ac.uk/pdbsum/1bu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bu8 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/LIPR2_RAT LIPR2_RAT] Lipase with broad substrate specificity. Can hydrolyze both phospholipids and galactolipids. Shows a preference for 1,2-didodecanoylphosphatidylethanolamine and 1,2-didodecanoylphosphatidylglycerol, and has low activity towards 1,2-didodecanoylphosphatidylcholine (in vitro).<ref>PMID:9822688</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 16:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bu8 ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bu8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The pancreas expresses several members of the lipase gene family including pancreatic triglyceride lipase (PTL) and two homologous proteins, pancreatic lipase-related proteins 1 and 2 (PLRP1 and PLRP2). Despite their similar amino acid sequences, PTL, PLRP1, and PLRP2 differ in important kinetic properties. PLRP1 has no known activity. PTL and PLRP2 differ in substrate specificity, bile acid inhibition, colipase requirement, and interfacial activation. To begin understanding the structural explanations for these functional differences, we solved the crystal structure of rat (r)PLRP2 and further characterized its kinetic properties. The 1.8 A structure of rPLRP2, like the tertiary structure of human PTL, has a globular N-terminal domain and a beta-sandwich C-terminal domain. The lid domain occupied the closed position, suggesting that rPLRP2 should show interfacial activation. When we reexamined this issue with tripropionin as substrate, rPLRP2 exhibited interfacial activation. Because the active site topology of rPLRP2 resembled that of human PTL, we predicted and demonstrated that the lipase inhibitors E600 and tetrahydrolipstatin inhibit rPLRP2. Although PTL and rPLRP2 have similar active sites, rPLRP2 has a broader substrate specificity that we confirmed using a monolayer technique. With this assay, we showed for the first time that rPLRP2 prefers phosphatidylglycerol and ethanolamine over phosphatidylcholine. In summary, we confirmed and extended the observation that PLRP2 lipases have a broader substrate specificity than PTL, we demonstrated that PLRP2 lipases show interfacial activation, and we solved the first crystal structure of a PLRP2 lipase that contains a lid domain.
		+
		+	Structure and activity of rat pancreatic lipase-related protein 2.,Roussel A, Yang Y, Ferrato F, Verger R, Cambillau C, Lowe M J Biol Chem. 1998 Nov 27;273(48):32121-8. PMID:9822688<ref>PMID:9822688</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1bu8" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Rattus norvegicus]]
	[[Category: Cambillau C]]		[[Category: Cambillau C]]
	[[Category: Roussel A]]		[[Category: Roussel A]]

OCA at 15:12, 3 March 2021

OCA — Wed, 03 Mar 2021 15:12:20 GMT

←Older revision		Revision as of 15:12, 3 March 2021
Line 1:		Line 1:

	==RAT PANCREATIC LIPASE RELATED PROTEIN 2==		==RAT PANCREATIC LIPASE RELATED PROTEIN 2==
-	<StructureSection load='1bu8' size='340' side='right'caption='[[1bu8]]~~, [[Resolution\|resolution]] 1.80Å~~' scene=''>	+	<StructureSection load='1bu8' size='340' side='right'caption='[[1bu8]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[1bu8]] is a 1 chain structure.~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>
-	</td></tr>~~<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>~~	+	</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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [https://pdbe.org/1bu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [https://www.ebi.ac.uk/pdbsum/1bu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bu8 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [~~http~~://pdbe.org/1bu8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1bu8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1bu8 ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[http://www.uniprot.org/uniprot/LIPR2_RAT LIPR2_RAT]] Lipase with broad substrate specificity. Can hydrolyze both phospholipids and galactolipids. Shows a preference for 1,2-didodecanoylphosphatidylethanolamine and 1,2-didodecanoylphosphatidylglycerol, and has low activity towards 1,2-didodecanoylphosphatidylcholine (in vitro).<ref>PMID:9822688</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 16:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bu8 ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bu8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The pancreas expresses several members of the lipase gene family including pancreatic triglyceride lipase (PTL) and two homologous proteins, pancreatic lipase-related proteins 1 and 2 (PLRP1 and PLRP2). Despite their similar amino acid sequences, PTL, PLRP1, and PLRP2 differ in important kinetic properties. PLRP1 has no known activity. PTL and PLRP2 differ in substrate specificity, bile acid inhibition, colipase requirement, and interfacial activation. To begin understanding the structural explanations for these functional differences, we solved the crystal structure of rat (r)PLRP2 and further characterized its kinetic properties. The 1.8 A structure of rPLRP2, like the tertiary structure of human PTL, has a globular N-terminal domain and a beta-sandwich C-terminal domain. The lid domain occupied the closed position, suggesting that rPLRP2 should show interfacial activation. When we reexamined this issue with tripropionin as substrate, rPLRP2 exhibited interfacial activation. Because the active site topology of rPLRP2 resembled that of human PTL, we predicted and demonstrated that the lipase inhibitors E600 and tetrahydrolipstatin inhibit rPLRP2. Although PTL and rPLRP2 have similar active sites, rPLRP2 has a broader substrate specificity that we confirmed using a monolayer technique. With this assay, we showed for the first time that rPLRP2 prefers phosphatidylglycerol and ethanolamine over phosphatidylcholine. In summary, we confirmed and extended the observation that PLRP2 lipases have a broader substrate specificity than PTL, we demonstrated that PLRP2 lipases show interfacial activation, and we solved the first crystal structure of a PLRP2 lipase that contains a lid domain.
-
-	Structure and activity of rat pancreatic lipase-related protein 2.,Roussel A, Yang Y, Ferrato F, Verger R, Cambillau C, Lowe M J Biol Chem. 1998 Nov 27;273(48):32121-8. PMID:9822688<ref>PMID:9822688</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1bu8" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Triacylglycerol lipase]]~~	+	[[Category: Cambillau C]]
-	[[Category: Cambillau, C]]	+	[[Category: Roussel A]]
-	[[Category: Roussel, A]]	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Lipid degradation]]~~	+
-	~~[[Category: Pancreatic lipase~~]]	+

OCA at 08:32, 21 May 2019

OCA — Tue, 21 May 2019 08:32:31 GMT

←Older revision		Revision as of 08:32, 21 May 2019
Line 1:		Line 1:

	==RAT PANCREATIC LIPASE RELATED PROTEIN 2==		==RAT PANCREATIC LIPASE RELATED PROTEIN 2==
-	<StructureSection load='1bu8' size='340' side='right' caption='[[1bu8]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='1bu8' size='340' side='right'caption='[[1bu8]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1bu8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1bu8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/1bu8_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/1bu8_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 33:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Triacylglycerol lipase]]		[[Category: Triacylglycerol lipase]]
	[[Category: Cambillau, C]]		[[Category: Cambillau, C]]

OCA at 06:00, 17 August 2017

OCA — Thu, 17 Aug 2017 06:00:57 GMT

←Older revision		Revision as of 06:00, 17 August 2017
Line 1:		Line 1:
		+
	==RAT PANCREATIC LIPASE RELATED PROTEIN 2==		==RAT PANCREATIC LIPASE RELATED PROTEIN 2==
	<StructureSection load='1bu8' size='340' side='right' caption='[[1bu8]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1bu8' size='340' side='right' caption='[[1bu8]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1bu8]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1bu8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [http://pdbe.org/1bu8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bu8 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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [http://pdbe.org/1bu8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bu8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bu8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bu8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 32:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
	[[Category: Triacylglycerol lipase]]		[[Category: Triacylglycerol lipase]]
	[[Category: Cambillau, C]]		[[Category: Cambillau, C]]

OCA at 13:27, 11 September 2015

OCA — Fri, 11 Sep 2015 13:27:50 GMT

←Older revision		Revision as of 13:27, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1bu8' size='340' side='right' caption='[[1bu8]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1bu8' size='340' side='right' caption='[[1bu8]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1bu8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1bu8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bu8 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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [http://pdbe.org/1bu8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bu8 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	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 1bu8" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Rattus norvegicus~~]]	+	[[Category: Buffalo rat]]
	[[Category: Triacylglycerol lipase]]		[[Category: Triacylglycerol lipase]]
	[[Category: Cambillau, C]]		[[Category: Cambillau, C]]

OCA at 17:04, 25 December 2014

OCA — Thu, 25 Dec 2014 17:04:28 GMT

←Older revision		Revision as of 17:04, 25 December 2014
Line 7:		Line 7:
	<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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bu8 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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bu8 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/LIPR2_RAT LIPR2_RAT]] Lipase with broad substrate specificity. Can hydrolyze both phospholipids and galactolipids. Shows a preference for 1,2-didodecanoylphosphatidylethanolamine and 1,2-didodecanoylphosphatidylglycerol, and has low activity towards 1,2-didodecanoylphosphatidylcholine (in vitro).<ref>PMID:9822688</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:26, 22 December 2014

OCA — Mon, 22 Dec 2014 08:26:13 GMT

←Older revision		Revision as of 08:26, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1bu8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1bu8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bu8 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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bu8 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Triacylglycerol lipase]]		[[Category: Triacylglycerol lipase]]
-	[[Category: Cambillau, C.]]	+	[[Category: Cambillau, C]]
-	[[Category: Roussel, A.]]	+	[[Category: Roussel, A]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Lipid degradation]]		[[Category: Lipid degradation]]
	[[Category: Pancreatic lipase]]		[[Category: Pancreatic lipase]]

OCA at 09:33, 13 August 2014

OCA — Wed, 13 Aug 2014 09:33:47 GMT

←Older revision		Revision as of 09:33, 13 August 2014
Line 1:		Line 1:
-	[[~~Image~~:1bu8.~~png\|left~~\|200px]]	+	==RAT PANCREATIC LIPASE RELATED PROTEIN 2==
		+	<StructureSection load='1bu8' size='340' side='right' caption='[[1bu8]], [[Resolution\|resolution]] 1.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1bu8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BU8 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </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=1bu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bu8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bu8 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/1bu8_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The pancreas expresses several members of the lipase gene family including pancreatic triglyceride lipase (PTL) and two homologous proteins, pancreatic lipase-related proteins 1 and 2 (PLRP1 and PLRP2). Despite their similar amino acid sequences, PTL, PLRP1, and PLRP2 differ in important kinetic properties. PLRP1 has no known activity. PTL and PLRP2 differ in substrate specificity, bile acid inhibition, colipase requirement, and interfacial activation. To begin understanding the structural explanations for these functional differences, we solved the crystal structure of rat (r)PLRP2 and further characterized its kinetic properties. The 1.8 A structure of rPLRP2, like the tertiary structure of human PTL, has a globular N-terminal domain and a beta-sandwich C-terminal domain. The lid domain occupied the closed position, suggesting that rPLRP2 should show interfacial activation. When we reexamined this issue with tripropionin as substrate, rPLRP2 exhibited interfacial activation. Because the active site topology of rPLRP2 resembled that of human PTL, we predicted and demonstrated that the lipase inhibitors E600 and tetrahydrolipstatin inhibit rPLRP2. Although PTL and rPLRP2 have similar active sites, rPLRP2 has a broader substrate specificity that we confirmed using a monolayer technique. With this assay, we showed for the first time that rPLRP2 prefers phosphatidylglycerol and ethanolamine over phosphatidylcholine. In summary, we confirmed and extended the observation that PLRP2 lipases have a broader substrate specificity than PTL, we demonstrated that PLRP2 lipases show interfacial activation, and we solved the first crystal structure of a PLRP2 lipase that contains a lid domain.

-	~~{{STRUCTURE_1bu8\| PDB=1bu8 \| SCENE= }}~~	+	Structure and activity of rat pancreatic lipase-related protein 2.,Roussel A, Yang Y, Ferrato F, Verger R, Cambillau C, Lowe M J Biol Chem. 1998 Nov 27;273(48):32121-8. PMID:9822688<ref>PMID:9822688</ref>

-	~~===RAT PANCREATIC LIPASE RELATED PROTEIN 2===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9822688}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1bu8]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Rattus_norvegicus Rattus norvegicus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:009822688<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Triacylglycerol lipase]]		[[Category: Triacylglycerol lipase]]

OCA: Protected "1bu8" [edit=sysop:move=sysop]

OCA — Sun, 21 Oct 2012 19:57:29 GMT

Protected "1bu8" [edit=sysop:move=sysop]

←Older revision

Revision as of 19:57, 21 October 2012

OCA at 19:57, 21 October 2012

OCA — Sun, 21 Oct 2012 19:57:25 GMT

←Older revision		Revision as of 19:57, 21 October 2012
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-	{{Seed}}
	[[Image:1bu8.png\|left\|200px]]		[[Image:1bu8.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1bu8", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1bu8\| PDB=1bu8 \| SCENE= }}		{{STRUCTURE_1bu8\| PDB=1bu8 \| SCENE= }}

	===RAT PANCREATIC LIPASE RELATED PROTEIN 2===		===RAT PANCREATIC LIPASE RELATED PROTEIN 2===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_9822688}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 9822688 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_9822688}}		{{ABSTRACT_PUBMED_9822688}}

	==About this Structure==		==About this Structure==
-	~~1BU8~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA].	+	[[1bu8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU8 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~9822688~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:009822688</ref><references group="xtra"/>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Triacylglycerol lipase]]		[[Category: Triacylglycerol lipase]]
Line 31:		Line 19:
	[[Category: Lipid degradation]]		[[Category: Lipid degradation]]
	[[Category: Pancreatic lipase]]		[[Category: Pancreatic lipase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 23:06:26 2009''