6ob0: Difference between revisions

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'''Unreleased structure'''


The entry 6ob0 is ON HOLD until Paper Publication
==Compound 2 bound structure of WT Lipoprotein Lipase in Complex with GPIHBP1 Mutant N78D N82D produced in HEK293-F cells==
 
<StructureSection load='6ob0' size='340' side='right'caption='[[6ob0]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6ob0]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OB0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OB0 FirstGlance]. <br>
Description:  
</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=M3D:7-(3-cyano-4-hydroxyphenyl)-N-[2-(morpholin-4-yl)ethyl]dibenzo[b,f]oxepine-10-carboxamide'>M3D</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
[[Category: Unreleased Structures]]
<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>
<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=6ob0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ob0 OCA], [http://pdbe.org/6ob0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ob0 RCSB], [http://www.ebi.ac.uk/pdbsum/6ob0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ob0 ProSAT]</span></td></tr>
</table>
== Disease ==
[[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.
== Function ==
[[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).
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lipoprotein lipase]]
[[Category: Arora, R]]
[[Category: Benson, T E]]
[[Category: Horton, P A]]
[[Category: Romanowski, M J]]
[[Category: Hydrolase-protein binding complex]]
[[Category: Lipase]]

Revision as of 14:23, 10 May 2019

Compound 2 bound structure of WT Lipoprotein Lipase in Complex with GPIHBP1 Mutant N78D N82D produced in HEK293-F cellsCompound 2 bound structure of WT Lipoprotein Lipase in Complex with GPIHBP1 Mutant N78D N82D produced in HEK293-F cells

Structural highlights

6ob0 is a 8 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Activity:Lipoprotein lipase, with EC number 3.1.1.34
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[LIPL_HUMAN] Hyperlipoproteinemia type 5;Familial lipoprotein lipase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [HDBP1_HUMAN] Familial chylomicronemia syndrome. The disease is caused by mutations affecting the gene represented in this entry.

Function

[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).[1] [2] [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).

References

  1. ↑ Lutz EP, Merkel M, Kako Y, Melford K, Radner H, Breslow JL, Bensadoun A, Goldberg IJ. Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues. J Clin Invest. 2001 May;107(9):1183-92. doi: 10.1172/JCI11774. PMID:11342582 doi:http://dx.doi.org/10.1172/JCI11774
  2. ↑ Pingitore P, Lepore SM, Pirazzi C, Mancina RM, Motta BM, Valenti L, Berge KE, Retterstol K, Leren TP, Wiklund O, Romeo S. Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia. J Clin Lipidol. 2016 Jul-Aug;10(4):816-823. doi: 10.1016/j.jacl.2016.02.015. Epub, 2016 Mar 10. PMID:27578112 doi:http://dx.doi.org/10.1016/j.jacl.2016.02.015

6ob0, resolution 2.81Å

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OCA
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