3rwv

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<StructureSection load='3rwv' size='340' side='right'caption='[[3rwv]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='3rwv' size='340' side='right'caption='[[3rwv]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rwv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RWV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rwv]] 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=3RWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RWV FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2evt|2evt]], [[1swx|1swx]], [[3rzn|3rzn]], [[3s0i|3s0i]], [[3s0k|3s0k]], [[3ric|3ric]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLTP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rwv OCA], [https://pdbe.org/3rwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rwv RCSB], [https://www.ebi.ac.uk/pdbsum/3rwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rwv 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=3rwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rwv OCA], [https://pdbe.org/3rwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rwv RCSB], [https://www.ebi.ac.uk/pdbsum/3rwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rwv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human glycolipid transfer protein (GLTP) fold represents a novel structural motif for lipid binding/transfer and reversible membrane translocation. GLTPs transfer glycosphingolipids (GSLs) that are key regulators of cell growth, division, surface adhesion, and neurodevelopment. Herein, we report structure-guided engineering of the lipid binding features of GLTP. New crystal structures of wild-type GLTP and two mutants (D48V and A47D ||D48V), each containing bound N-nervonoyl-sulfatide, reveal the molecular basis for selective anchoring of sulfatide (3-O-sulfo-galactosylceramide) by D48V-GLTP. Directed point mutations of "portal entrance" residues, A47 and D48, reversibly regulate sphingosine access to the hydrophobic pocket via a mechanism that could involve homodimerization. "Door-opening" conformational changes by phenylalanines within the hydrophobic pocket are revealed during lipid encapsulation by new crystal structures of bona fide apo-GLTP and GLTP complexed with N-oleoyl-glucosylceramide. The development of "engineered GLTPs" with enhanced specificity for select GSLs provides a potential new therapeutic approach for targeting GSL-mediated pathologies.
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Enhanced selectivity for sulfatide by engineered human glycolipid transfer protein.,Samygina VR, Popov AN, Cabo-Bilbao A, Ochoa-Lizarralde B, Goni-de-Cerio F, Zhai X, Molotkovsky JG, Patel DJ, Brown RE, Malinina L Structure. 2011 Nov 9;19(11):1644-54. PMID:22078563<ref>PMID:22078563</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3rwv" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Brown, R E]]
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[[Category: Brown RE]]
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[[Category: Cabo-Bilbao, A]]
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[[Category: Cabo-Bilbao A]]
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[[Category: Goni-de-Cerio, F]]
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[[Category: Goni-de-Cerio F]]
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[[Category: Malinina, L]]
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[[Category: Malinina L]]
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[[Category: Ochoa-Lizarralde, B]]
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[[Category: Ochoa-Lizarralde B]]
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[[Category: Patel, D J]]
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[[Category: Patel DJ]]
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[[Category: Popov, A N]]
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[[Category: Popov AN]]
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[[Category: Samygina, V]]
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[[Category: Samygina V]]
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[[Category: Gltp-fold]]
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[[Category: Lipid transport]]
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Current revision

Crystal Structure of apo-form of Human Glycolipid Transfer Protein at 1.5 A resolution

PDB ID 3rwv

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Proteopedia Page Contributors and Editors (what is this?)

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