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1lpa
From Proteopedia
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| - | [[Image:1lpa.png|left|200px]] | ||
| - | + | ==INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY== | |
| - | + | <StructureSection load='1lpa' size='340' side='right'caption='[[1lpa]], [[Resolution|resolution]] 3.04Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1lpa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LPA FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.04Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PLC:DIUNDECYL+PHOSPHATIDYL+CHOLINE'>PLC</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=1lpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpa OCA], [https://pdbe.org/1lpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lpa RCSB], [https://www.ebi.ac.uk/pdbsum/1lpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lpa ProSAT]</span></td></tr> |
| - | [[1lpa]] is a 2 chain structure with sequence from [ | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/COL_PIG COL_PIG] Colipase is a cofactor of pancreatic lipase. It allows the lipase to anchor itself to the lipid-water interface. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase. Enterostatin has a biological activity as a satiety signal. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lp/1lpa_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1lpa ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Lipase|Lipase]] | + | *[[Lipase 3D Structures|Lipase 3D Structures]] |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | + | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
| - | + | [[Category: Cambillau C]] | |
| - | [[Category: Cambillau | + | [[Category: Egloff M-P]] |
| - | [[Category: Egloff | + | [[Category: Van Tilbeurgh H]] |
| - | [[Category: Tilbeurgh | + | |
Current revision
INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY
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