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6oau

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'''Unreleased structure'''
 
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The entry 6oau is ON HOLD until Paper Publication
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==Apo Structure of WT Lipoprotein Lipase in Complex with GPIHBP1 Mutant N78D N82D produced in GnTI-deficient HEK293-F cells==
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<StructureSection load='6oau' size='340' side='right'caption='[[6oau]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6oau]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OAU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OAU FirstGlance]. <br>
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Description:
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lipoprotein_lipase Lipoprotein lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.34 3.1.1.34] </span></td></tr>
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<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=6oau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oau OCA], [http://pdbe.org/6oau PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oau RCSB], [http://www.ebi.ac.uk/pdbsum/6oau PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oau ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/LIPL_HUMAN LIPL_HUMAN]] Hyperlipoproteinemia type 5;Familial lipoprotein lipase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/HDBP1_HUMAN HDBP1_HUMAN]] Familial chylomicronemia syndrome. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[[http://www.uniprot.org/uniprot/LIPL_HUMAN LIPL_HUMAN]] The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL) (PubMed:27578112). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium (By similarity).<ref>PMID:11342582</ref> <ref>PMID:27578112</ref> [[http://www.uniprot.org/uniprot/HDBP1_HUMAN HDBP1_HUMAN]] Plays a key role in the lipolytic processing of chylomicrons. Required for the transport of lipoprotein lipase LPL into the capillary lumen (By similarity).
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Lipoprotein lipase]]
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[[Category: Arora, R]]
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[[Category: Benson, T E]]
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[[Category: Horton, P A]]
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[[Category: Romanowski, M J]]
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[[Category: Hydrolase-protein binding complex]]
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[[Category: Lipase]]

Revision as of 11:23, 10 May 2019

Apo Structure of WT Lipoprotein Lipase in Complex with GPIHBP1 Mutant N78D N82D produced in GnTI-deficient HEK293-F cells

PDB ID 6oau

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