2evs - Revision history

OCA at 07:40, 23 August 2023

2023-08-23T07:40:24Z

← Older revision		Revision as of 07:40, 23 August 2023
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	==Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside==		==Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside==
	<StructureSection load='2evs' size='340' side='right'caption='[[2evs]]' scene=''>		<StructureSection load='2evs' size='340' side='right'caption='[[2evs]], [[Resolution\|resolution]] 2.20Å' 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=2EVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EVS FirstGlance]. <br>		<table><tr><td colspan='2'>[[2evs]] is a 2 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=2EVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EVS 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=2evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evs OCA], [https://pdbe.org/2evs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2evs RCSB], [https://www.ebi.ac.uk/pdbsum/2evs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2evs 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]] 2.2Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</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=2evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evs OCA], [https://pdbe.org/2evs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2evs RCSB], [https://www.ebi.ac.uk/pdbsum/2evs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2evs ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[https://www.uniprot.org/uniprot/GLTP_HUMAN GLTP_HUMAN] Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides.<ref>PMID:18261224</ref> <ref>PMID:15504043</ref> <ref>PMID:17980653</ref> <ref>PMID:15329726</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=2evs 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=2evs ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Glycosphingolipids (GSLs) play major roles in cellular growth and development. Mammalian glycolipid transfer proteins (GLTPs) are potential regulators of cell processes mediated by GSLs and display a unique architecture among lipid binding/transfer proteins. The GLTP fold represents a novel membrane targeting/interaction domain among peripheral proteins. Here we report crystal structures of human GLTP bound to GSLs of diverse acyl chain length, unsaturation, and sugar composition. Structural comparisons show a highly conserved anchoring of galactosyl- and lactosyl-amide headgroups by the GLTP recognition center. By contrast, acyl chain chemical structure and occupancy of the hydrophobic tunnel dictate partitioning between sphingosine-in and newly-observed sphingosine-out ligand-binding modes. The structural insights, combined with computed interaction propensity distributions, suggest a concerted sequence of events mediated by GLTP conformational changes during GSL transfer to and/or from membranes, as well as during GSL presentation and/or transfer to other proteins.

			The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure.,Malinina L, Malakhova ML, Kanack AT, Lu M, Abagyan R, Brown RE, Patel DJ PLoS Biol. 2006 Nov;4(11):e362. PMID:17105344<ref>PMID:17105344</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 2evs" style="background-color:#fffaf0;"></div>
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Abagyan R]]		[[Category: Abagyan R]]

OCA at 10:36, 17 February 2021

2021-02-17T10:36:35Z

← Older revision		Revision as of 10:36, 17 February 2021
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	==Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside==		==Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside==
	<StructureSection load='2evs' size='340' side='right' caption='[[2evs]]~~, [[Resolution\|resolution]] 2.20Å~~' scene=''>		<StructureSection load='2evs' size='340' side='right'caption='[[2evs]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>~~[[2evs]] is a 2 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=2EVS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2EVS FirstGlance]. <br>		<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EVS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</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=2evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evs OCA], [https://pdbe.org/2evs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2evs RCSB], [https://www.ebi.ac.uk/pdbsum/2evs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2evs ProSAT]</span></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1swx\|1swx]]</td></tr>~~
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GLTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evs OCA], [~~http~~://pdbe.org/2evs PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2evs RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2evs PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2evs ProSAT]</span></td></tr>
	</table>		</table>
	~~== Function ==~~
	[[http://www.uniprot.org/uniprot/GLTP_HUMAN GLTP_HUMAN]] Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides.<ref>PMID:18261224</ref> <ref>PMID:15504043</ref> <ref>PMID:17980653</ref> <ref>PMID:15329726</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ev/2evs_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ev/2evs_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 21:		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=2evs 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=2evs ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Glycosphingolipids (GSLs) play major roles in cellular growth and development. Mammalian glycolipid transfer proteins (GLTPs) are potential regulators of cell processes mediated by GSLs and display a unique architecture among lipid binding/transfer proteins. The GLTP fold represents a novel membrane targeting/interaction domain among peripheral proteins. Here we report crystal structures of human GLTP bound to GSLs of diverse acyl chain length, unsaturation, and sugar composition. Structural comparisons show a highly conserved anchoring of galactosyl- and lactosyl-amide headgroups by the GLTP recognition center. By contrast, acyl chain chemical structure and occupancy of the hydrophobic tunnel dictate partitioning between sphingosine-in and newly-observed sphingosine-out ligand-binding modes. The structural insights, combined with computed interaction propensity distributions, suggest a concerted sequence of events mediated by GLTP conformational changes during GSL transfer to and/or from membranes, as well as during GSL presentation and/or transfer to other proteins.

	The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure.,Malinina L, Malakhova ML, Kanack AT, Lu M, Abagyan R, Brown RE, Patel DJ PLoS Biol. 2006 Nov;4(11):e362. PMID:17105344<ref>PMID:17105344</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2evs" style="background-color:#fffaf0;"></div>~~
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Large Structures]]
	[[Category: Abagyan, R]]		[[Category: Abagyan R]]
	[[Category: Brown~~, R E~~]]		[[Category: Brown RE]]
	[[Category: Kanack~~, A T~~]]		[[Category: Kanack AT]]
	[[Category: Malakhova~~, M L~~]]		[[Category: Malakhova ML]]
	[[Category: Malinina, L]]		[[Category: Malinina L]]
	[[Category: Patel~~, D J]]~~		[[Category: Patel DJ]]
	~~[[Category: Lipid transport]]~~
	~~[[Category: Protein complex with detergent~~]]

OCA at 07:29, 18 October 2017

2017-10-18T07:29:20Z

← Older revision		Revision as of 07:29, 18 October 2017
Line 1:		Line 1:

	==Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside==		==Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside==
	<StructureSection load='2evs' size='340' side='right' caption='[[2evs]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2evs' size='340' side='right' caption='[[2evs]], [[Resolution\|resolution]] 2.20Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1swx\|1swx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1swx\|1swx]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GLTP ([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">GLTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evs OCA], [http://pdbe.org/2evs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2evs RCSB], [http://www.ebi.ac.uk/pdbsum/2evs 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=2evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evs OCA], [http://pdbe.org/2evs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2evs RCSB], [http://www.ebi.ac.uk/pdbsum/2evs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2evs ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	<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=2evs ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 15:55, 11 September 2015

2015-09-11T15:55:26Z

← Older revision		Revision as of 15:55, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2evs' size='340' side='right' caption='[[2evs]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2evs' size='340' side='right' caption='[[2evs]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2evs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EVS FirstGlance]. <br>		<table><tr><td colspan='2'>[[2evs]] is a 2 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=2EVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EVS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1swx\|1swx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1swx\|1swx]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GLTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GLTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2evs RCSB], [http://www.ebi.ac.uk/pdbsum/2evs 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=2evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evs OCA], [http://pdbe.org/2evs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2evs RCSB], [http://www.ebi.ac.uk/pdbsum/2evs PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 2evs" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Abagyan, R]]		[[Category: Abagyan, R]]
	[[Category: Brown, R E]]		[[Category: Brown, R E]]

OCA at 18:40, 25 December 2014

2014-12-25T18:40:18Z

← Older revision		Revision as of 18:40, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2evs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EVS FirstGlance]. <br>		<table><tr><td colspan='2'>[[2evs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EVS FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1swx\|1swx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1swx\|1swx]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GLTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GLTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2evs RCSB], [http://www.ebi.ac.uk/pdbsum/2evs 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=2evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2evs RCSB], [http://www.ebi.ac.uk/pdbsum/2evs PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/GLTP_HUMAN GLTP_HUMAN]] Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides.<ref>PMID:18261224</ref> <ref>PMID:15504043</ref> <ref>PMID:17980653</ref> <ref>PMID:15329726</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Abagyan, R.]]		[[Category: Abagyan, R]]
	[[Category: Brown, R E.]]		[[Category: Brown, R E]]
	[[Category: Kanack, A T.]]		[[Category: Kanack, A T]]
	[[Category: Malakhova, M L.]]		[[Category: Malakhova, M L]]
	[[Category: Malinina, L.]]		[[Category: Malinina, L]]
	[[Category: Patel, D J.]]		[[Category: Patel, D J]]
	[[Category: Lipid transport]]		[[Category: Lipid transport]]
	[[Category: Protein complex with detergent]]		[[Category: Protein complex with detergent]]

OCA at 02:31, 30 September 2014

2014-09-30T02:31:43Z

← Older revision		Revision as of 02:31, 30 September 2014
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	[[Image:~~2evs~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside==
			<StructureSection load='2evs' size='340' side='right' caption='[[2evs]], [[Resolution\|resolution]] 2.20Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2evs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EVS FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1swx\|1swx]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GLTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2evs RCSB], [http://www.ebi.ac.uk/pdbsum/2evs 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/ev/2evs_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 ==
			Glycosphingolipids (GSLs) play major roles in cellular growth and development. Mammalian glycolipid transfer proteins (GLTPs) are potential regulators of cell processes mediated by GSLs and display a unique architecture among lipid binding/transfer proteins. The GLTP fold represents a novel membrane targeting/interaction domain among peripheral proteins. Here we report crystal structures of human GLTP bound to GSLs of diverse acyl chain length, unsaturation, and sugar composition. Structural comparisons show a highly conserved anchoring of galactosyl- and lactosyl-amide headgroups by the GLTP recognition center. By contrast, acyl chain chemical structure and occupancy of the hydrophobic tunnel dictate partitioning between sphingosine-in and newly-observed sphingosine-out ligand-binding modes. The structural insights, combined with computed interaction propensity distributions, suggest a concerted sequence of events mediated by GLTP conformational changes during GSL transfer to and/or from membranes, as well as during GSL presentation and/or transfer to other proteins.

	~~{{STRUCTURE_2evs\| PDB=2evs \| SCENE= }}~~		The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure.,Malinina L, Malakhova ML, Kanack AT, Lu M, Abagyan R, Brown RE, Patel DJ PLoS Biol. 2006 Nov;4(11):e362. PMID:17105344<ref>PMID:17105344</ref>

	~~===Crystal structure~~ of ~~human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_17105344}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[2evs]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2EVS OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:017105344<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Abagyan, R.]]		[[Category: Abagyan, R.]]

OCA: Protected "2evs" [edit=sysop:move=sysop]

2013-01-06T11:43:58Z

Protected "2evs" [edit=sysop:move=sysop]

← Older revision	Revision as of 11:43, 6 January 2013
(No difference)

OCA at 11:43, 6 January 2013

2013-01-06T11:43:56Z

← Older revision		Revision as of 11:43, 6 January 2013
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	~~{{Seed}}~~
	[[Image:2evs.png\|left\|200px]]		[[Image:2evs.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2evs", 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_2evs\| PDB=2evs \| SCENE= }}		{{STRUCTURE_2evs\| PDB=2evs \| SCENE= }}

	===Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside===		===Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_17105344}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 17105344 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_17105344}}		{{ABSTRACT_PUBMED_17105344}}

	==About this Structure==		==About this Structure==
	~~2EVS~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVS OCA].		[[2evs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVS OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~17105344~~</ref><references group="xtra"/>		<ref group="xtra">PMID:017105344</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Abagyan, R.]]		[[Category: Abagyan, R.]]
Line 31:		Line 19:
	[[Category: Malinina, L.]]		[[Category: Malinina, L.]]
	[[Category: Patel, D J.]]		[[Category: Patel, D J.]]
			[[Category: Lipid transport]]
	[[Category: Protein complex with detergent]]		[[Category: Protein complex with detergent]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:47:26 2009''~~

OCA at 00:47, 18 February 2009

2009-02-18T00:47:29Z

← Older revision		Revision as of 00:47, 18 February 2009
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	==About this Structure==		==About this Structure==
	2EVS is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVS OCA].		2EVS is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVS OCA].

	==Reference==		==Reference==
	~~The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure., Malinina L, Malakhova ML, Kanack AT, Lu M, Abagyan R, Brown RE, Patel DJ, PLoS Biol. 2006 Nov;4(11):e362.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/17105344 17105344]~~		<ref group="xtra">PMID:17105344</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	~~[[Category: Single protein]]~~
	[[Category: Abagyan, R.]]		[[Category: Abagyan, R.]]
	[[Category: Brown, R E.]]		[[Category: Brown, R E.]]
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	[[Category: Protein complex with detergent]]		[[Category: Protein complex with detergent]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jul 29 09~~:27:~~39 2008~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:47:26 2009''

OCA at 06:27, 29 July 2008

2008-07-29T06:27:41Z

← Older revision		Revision as of 06:27, 29 July 2008
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	[[Image:2evs.~~gif~~\|left\|200px]]		{{Seed}}
			[[Image:2evs.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_2evs\| PDB=2evs \| SCENE= }}		{{STRUCTURE_2evs\| PDB=2evs \| SCENE= }}

	~~'''~~Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside~~'''~~		===Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside===


	~~==Overview==~~		<!--
	~~Glycosphingolipids~~ (GSLs) play major roles in cellular growth and development. Mammalian glycolipid transfer proteins (GLTPs) are potential regulators of cell processes mediated by GSLs and display a unique architecture among lipid binding/~~transfer proteins~~. ~~The GLTP fold represents a novel membrane targeting/interaction domain among peripheral proteins~~. ~~Here we report crystal structures of human GLTP bound to GSLs of diverse acyl chain length~~, ~~unsaturation, and sugar composition. Structural comparisons show a highly conserved anchoring of galactosyl- and lactosyl-amide headgroups by~~ the ~~GLTP recognition center~~. ~~By contrast, acyl chain chemical structure and occupancy of the hydrophobic tunnel dictate partitioning between sphingosine~~-~~in and newly~~-observed sphingosine-out ligand-binding modes. The structural insights, combined with computed interaction propensity distributions, suggest a concerted sequence of events mediated by GLTP conformational changes during GSL transfer to and/or from membranes, as well as during GSL presentation and/or transfer to other proteins.		The line below this paragraph, {{ABSTRACT_PUBMED_17105344}}, adds the Publication Abstract to the page
			(as it appears on PubMed at http://www.pubmed.gov), where 17105344 is the PubMed ID number.
			-->
			{{ABSTRACT_PUBMED_17105344}}

	==About this Structure==		==About this Structure==
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	[[Category: Patel, D J.]]		[[Category: Patel, D J.]]
	[[Category: Protein complex with detergent]]		[[Category: Protein complex with detergent]]
	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 03~~:10:12 2008''
			''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:27:39 2008''