4gxd - Revision history

OCA at 08:51, 20 March 2024

OCA — Wed, 20 Mar 2024 08:51:40 GMT

←Older revision		Revision as of 08:51, 20 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gxd]] 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=4GXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GXD FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gxd]] 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=4GXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GXD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0SG:N-{(2S,3R,4E)-1-[(3,6-DI-O-SULFO-BETA-D-GALACTOPYRANOSYL)OXY]-3-HYDROXYOCTADEC-4-EN-2-YL}DODECANAMIDE'>0SG</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.1Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0SG:N-{(2S,3R,4E)-1-[(3,6-DI-O-SULFO-BETA-D-GALACTOPYRANOSYL)OXY]-3-HYDROXYOCTADEC-4-EN-2-YL}DODECANAMIDE'>0SG</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=4gxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxd OCA], [https://pdbe.org/4gxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gxd RCSB], [https://www.ebi.ac.uk/pdbsum/4gxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxd 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=4gxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxd OCA], [https://pdbe.org/4gxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gxd RCSB], [https://www.ebi.ac.uk/pdbsum/4gxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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>		[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>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Human glycolipid transfer protein (hsGLTP) forms the prototypical GLTP fold and is characterized by a broad transfer selectivity for glycosphingolipids (GSLs). The GLTP mutation D48V near the `portal entrance' of the glycolipid binding site has recently been shown to enhance selectivity for sulfatides (SFs) containing a long acyl chain. Here, nine novel crystal structures of hsGLTP and the SF-selective mutant complexed with short-acyl-chain monoSF and diSF in different crystal forms are reported in order to elucidate the potential functional roles of lipid-mediated homodimerization. In all crystal forms, the hsGLTP-SF complexes displayed homodimeric structures supported by similarly organized intermolecular interactions. The dimerization interface always involved the lipid sphingosine chain, the protein C-terminus (C-end) and alpha-helices 6 and 2, but the D48V mutant displayed a `locked' dimer conformation compared with the hinge-like flexibility of wild-type dimers. Differences in contact angles, areas and residues at the dimer interfaces in the `flexible' and `locked' dimers revealed a potentially important role of the dimeric structure in the C-end conformation of hsGLTP and in the precise positioning of the key residue of the glycolipid recognition centre, His140. DeltaY207 and DeltaC-end deletion mutants, in which the C-end is shifted or truncated, showed an almost complete loss of transfer activity. The new structural insights suggest that ligand-dependent reversible dimerization plays a role in the function of human GLTP.
-
-	Structural insights into lipid-dependent reversible dimerization of human GLTP.,Samygina VR, Ochoa-Lizarralde B, Popov AN, Cabo-Bilbao A, Goni-de-Cerio F, Molotkovsky JG, Patel DJ, Brown RE, Malinina L Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):603-16. doi:, 10.1107/S0907444913000024. Epub 2013 Mar 14. PMID:23519669<ref>PMID:23519669</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4gxd" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:24, 26 October 2022

OCA — Wed, 26 Oct 2022 07:24:26 GMT

←Older revision		Revision as of 07:24, 26 October 2022
Line 1:		Line 1:

	==Crystal structure of D48V mutant of human GLTP bound with 12:0 disulfatide==		==Crystal structure of D48V mutant of human GLTP bound with 12:0 disulfatide==
-	<StructureSection load='4gxd' size='340' side='right' caption='[[4gxd]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='4gxd' size='340' side='right'caption='[[4gxd]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gxd]] 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=4GXD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GXD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gxd]] 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=4GXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GXD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0SG:N-{(2S,3R,4E)-1-[(3,6-DI-O-SULFO-BETA-D-GALACTOPYRANOSYL)OXY]-3-HYDROXYOCTADEC-4-EN-2-YL}DODECANAMIDE'>0SG</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0SG:N-{(2S,3R,4E)-1-[(3,6-DI-O-SULFO-BETA-D-GALACTOPYRANOSYL)OXY]-3-HYDROXYOCTADEC-4-EN-2-YL}DODECANAMIDE'>0SG</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gvt\|4gvt]], [[4gix\|4gix]]</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=4gxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxd OCA], [https://pdbe.org/4gxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gxd RCSB], [https://www.ebi.ac.uk/pdbsum/4gxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxd ProSAT]</span></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=4gxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxd OCA], [~~http~~://pdbe.org/4gxd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gxd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gxd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxd ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== 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>	+	[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Malinina, L]]	+	[[Category: Large Structures]]
-	[[Category: Ochoa-Lizarralde, B]]	+	[[Category: Malinina L]]
-	[[Category: Popov~~, A N~~]]	+	[[Category: Ochoa-Lizarralde B]]
-	[[Category: Samygina~~, V R]]~~	+	[[Category: Popov AN]]
-	~~[[Category: Gltp-fold]]~~	+	[[Category: Samygina VR]]
-	~~[[Category: Lipid transport~~]]	+

OCA at 16:32, 4 August 2016

OCA — Thu, 04 Aug 2016 16:32:21 GMT

←Older revision		Revision as of 16:32, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of D48V mutant of human GLTP bound with 12:0 disulfatide==		==Crystal structure of D48V mutant of human GLTP bound with 12:0 disulfatide==
	<StructureSection load='4gxd' size='340' side='right' caption='[[4gxd]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4gxd' size='340' side='right' caption='[[4gxd]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gxd]] is a 1 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=4GXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GXD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gxd]] 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=4GXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GXD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0SG:N-{(2S,3R,4E)-1-[(3,6-DI-O-SULFO-BETA-D-GALACTOPYRANOSYL)OXY]-3-HYDROXYOCTADEC-4-EN-2-YL}DODECANAMIDE'>0SG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0SG:N-{(2S,3R,4E)-1-[(3,6-DI-O-SULFO-BETA-D-GALACTOPYRANOSYL)OXY]-3-HYDROXYOCTADEC-4-EN-2-YL}DODECANAMIDE'>0SG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gvt\|4gvt]], [[4gix\|4gix]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gvt\|4gvt]], [[4gix\|4gix]]</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=4gxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gxd RCSB], [http://www.ebi.ac.uk/pdbsum/4gxd 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=4gxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxd OCA], [http://pdbe.org/4gxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gxd RCSB], [http://www.ebi.ac.uk/pdbsum/4gxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4gxd" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Malinina, L]]		[[Category: Malinina, L]]
	[[Category: Ochoa-Lizarralde, B]]		[[Category: Ochoa-Lizarralde, B]]

OCA at 17:03, 24 December 2014

OCA — Wed, 24 Dec 2014 17:03:32 GMT

←Older revision		Revision as of 17:03, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4gxd\| PDB=4gxd \| SCENE= }}~~	+	==Crystal structure of D48V mutant of human GLTP bound with 12:0 disulfatide==
-	===Crystal structure of D48V mutant of human GLTP bound with 12:0 disulfatide===	+	<StructureSection load='4gxd' size='340' side='right' caption='[[4gxd]], [[Resolution\|resolution]] 2.10Å' scene=''>
-	{~~{ABSTRACT_PUBMED_23519669}~~}	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4gxd]] is a 1 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=4GXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GXD FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0SG:N-{(2S,3R,4E)-1-[(3,6-DI-O-SULFO-BETA-D-GALACTOPYRANOSYL)OXY]-3-HYDROXYOCTADEC-4-EN-2-YL}DODECANAMIDE'>0SG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gvt\|4gvt]], [[4gix\|4gix]]</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='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=4gxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gxd RCSB], [http://www.ebi.ac.uk/pdbsum/4gxd PDBsum]</span></td></tr>
		+	</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>		[[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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human glycolipid transfer protein (hsGLTP) forms the prototypical GLTP fold and is characterized by a broad transfer selectivity for glycosphingolipids (GSLs). The GLTP mutation D48V near the `portal entrance' of the glycolipid binding site has recently been shown to enhance selectivity for sulfatides (SFs) containing a long acyl chain. Here, nine novel crystal structures of hsGLTP and the SF-selective mutant complexed with short-acyl-chain monoSF and diSF in different crystal forms are reported in order to elucidate the potential functional roles of lipid-mediated homodimerization. In all crystal forms, the hsGLTP-SF complexes displayed homodimeric structures supported by similarly organized intermolecular interactions. The dimerization interface always involved the lipid sphingosine chain, the protein C-terminus (C-end) and alpha-helices 6 and 2, but the D48V mutant displayed a `locked' dimer conformation compared with the hinge-like flexibility of wild-type dimers. Differences in contact angles, areas and residues at the dimer interfaces in the `flexible' and `locked' dimers revealed a potentially important role of the dimeric structure in the C-end conformation of hsGLTP and in the precise positioning of the key residue of the glycolipid recognition centre, His140. DeltaY207 and DeltaC-end deletion mutants, in which the C-end is shifted or truncated, showed an almost complete loss of transfer activity. The new structural insights suggest that ligand-dependent reversible dimerization plays a role in the function of human GLTP.

-	~~==About this Structure==~~	+	Structural insights into lipid-dependent reversible dimerization of human GLTP.,Samygina VR, Ochoa-Lizarralde B, Popov AN, Cabo-Bilbao A, Goni-de-Cerio F, Molotkovsky JG, Patel DJ, Brown RE, Malinina L Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):603-16. doi:, 10.1107/S0907444913000024. Epub 2013 Mar 14. PMID:23519669<ref>PMID:23519669</ref>
-	~~[[4gxd]] is a 1 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=4GXD OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Malinina, L.]]	+	[[Category: Malinina, L]]
-	[[Category: Ochoa-Lizarralde, B.]]	+	[[Category: Ochoa-Lizarralde, B]]
-	[[Category: Popov, A N.]]	+	[[Category: Popov, A N]]
-	[[Category: Samygina, V R.]]	+	[[Category: Samygina, V R]]
	[[Category: Gltp-fold]]		[[Category: Gltp-fold]]
	[[Category: Lipid transport]]		[[Category: Lipid transport]]

OCA at 22:44, 10 April 2013

OCA — Wed, 10 Apr 2013 22:44:20 GMT

←Older revision		Revision as of 22:44, 10 April 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4gxd\| PDB=4gxd \| SCENE= }}
		+	===Crystal structure of D48V mutant of human GLTP bound with 12:0 disulfatide===
		+	{{ABSTRACT_PUBMED_23519669}}

-	~~The entry 4gxd is ON HOLD~~ ~~until Paper Publication~~	+	==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>

-	~~Authors~~: ~~Samygina, V~~.R.~~, Ochoa-Lizarralde, B~~.~~, Popov, A~~.N.~~, Malinina, L~~.	+	==About this Structure==
		+	[[4gxd]] is a 1 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=4GXD OCA].

-	~~Description~~: ~~Crystal structure of D48V mutant of human GLTP bound with 12~~:~~0 disulfatide~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Malinina, L.]]
		+	[[Category: Ochoa-Lizarralde, B.]]
		+	[[Category: Popov, A N.]]
		+	[[Category: Samygina, V R.]]
		+	[[Category: Gltp-fold]]
		+	[[Category: Lipid transport]]

OCA at 05:45, 3 October 2012

OCA — Wed, 03 Oct 2012 05:45:42 GMT

←Older revision		Revision as of 05:45, 3 October 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Samygina, V.R., Ochoa-Lizarralde, B., Popov, A.N., Malinina, L.		Authors: Samygina, V.R., Ochoa-Lizarralde, B., Popov, A.N., Malinina, L.

	Description: Crystal structure of D48V mutant of human GLTP bound with 12:0 disulfatide		Description: Crystal structure of D48V mutant of human GLTP bound with 12:0 disulfatide

OCA at 06:55, 19 September 2012

OCA — Wed, 19 Sep 2012 06:55:28 GMT

←Older revision		Revision as of 06:55, 19 September 2012
Line 3:		Line 3:
	The entry 4gxd is ON HOLD		The entry 4gxd is ON HOLD

-	Authors: Samygina, V. R., Ochoa-Lizarralde, B., Popov, A.N., Malinina, L.	+	Authors: Samygina, V.R., Ochoa-Lizarralde, B., Popov, A.N., Malinina, L.

	Description: Crystal structure of D48V mutant of human GLTP bound with 12:0 disulfatide		Description: Crystal structure of D48V mutant of human GLTP bound with 12:0 disulfatide

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

OCA — Wed, 12 Sep 2012 04:55:33 GMT

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

←Older revision

Revision as of 04:55, 12 September 2012

OCA: New page: '''Unreleased structure''' The entry 4gxd is ON HOLD Authors: Samygina, V. R., Ochoa-Lizarralde, B., Popov, A.N., Malinina, L. Description: Crystal structure of D48V mutant of human GL...

OCA — Wed, 12 Sep 2012 04:55:33 GMT

New page: '''Unreleased structure''' The entry 4gxd is ON HOLD Authors: Samygina, V. R., Ochoa-Lizarralde, B., Popov, A.N., Malinina, L. Description: Crystal structure of D48V mutant of human GL...

New page

'''Unreleased structure'''

The entry 4gxd is ON HOLD

Authors: Samygina, V. R., Ochoa-Lizarralde, B., Popov, A.N., Malinina, L.

Description: Crystal structure of D48V mutant of human GLTP bound with 12:0 disulfatide