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1gpl

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{{Seed}}
 
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[[Image:1gpl.png|left|200px]]
 
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<!--
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==RP2 LIPASE==
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The line below this paragraph, containing "STRUCTURE_1gpl", creates the "Structure Box" on the page.
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<StructureSection load='1gpl' size='340' side='right'caption='[[1gpl]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1gpl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cavia_porcellus Cavia porcellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GPL FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.01&#8491;</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=CA:CALCIUM+ION'>CA</scene></td></tr>
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{{STRUCTURE_1gpl| PDB=1gpl | SCENE= }}
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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=1gpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpl OCA], [https://pdbe.org/1gpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gpl RCSB], [https://www.ebi.ac.uk/pdbsum/1gpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gpl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIPP_HUMAN LIPP_HUMAN] [https://www.uniprot.org/uniprot/LIPR2_CAVPO LIPR2_CAVPO] Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:8490016, PubMed:17401110, PubMed:20083229, PubMed:8939760). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (By similarity). Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:8490016, PubMed:8939760). Can completely deacylate triacylglycerols (By similarity). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (PubMed:20083229, PubMed:8939760). Hydrolyzes medium- and long-chain fatty acyls in galactolipids. May act together with LIPF to hydrolyze partially digested triglycerides (By similarity). Hydrolyzes long-chain monoglycerides with high efficiency. In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity (By similarity). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity).[UniProtKB:P17892][UniProtKB:P54317][UniProtKB:P54318]<ref>PMID:17401110</ref> <ref>PMID:20083229</ref> <ref>PMID:8490016</ref> <ref>PMID:8939760</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/1gpl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1gpl ConSurf].
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<div style="clear:both"></div>
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===RP2 LIPASE===
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==See Also==
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_8993339}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 8993339 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_8993339}}
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==About this Structure==
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1GPL is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Cavia_porcellus Cavia porcellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPL OCA].
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==Reference==
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<ref group="xtra">PMID:8993339</ref><references group="xtra"/>
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[[Category: Cavia porcellus]]
[[Category: Cavia porcellus]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Large Structures]]
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[[Category: Cambillau, C.]]
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[[Category: Cambillau C]]
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[[Category: Withers-Martinez, C.]]
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[[Category: Withers-Martinez C]]
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[[Category: Chimeric]]
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[[Category: Glycoprotein]]
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[[Category: Hydrolase]]
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[[Category: Lipid degradation]]
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[[Category: Pancrea]]
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[[Category: Serine esterase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:22:36 2009''
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Current revision

RP2 LIPASE

PDB ID 1gpl

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