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1pco

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{{Seed}}
 
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[[Image:1pco.png|left|200px]]
 
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<!--
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==SOLUTION STRUCTURE OF PORCINE PANCREATIC PROCOLIPASE AS DETERMINED FROM 1H HOMONUCLEAR TWO-AND THREE-DIMENSIONAL NMR==
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The line below this paragraph, containing "STRUCTURE_1pco", creates the "Structure Box" on the page.
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<StructureSection load='1pco' size='340' side='right'caption='[[1pco]]' 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'>[[1pco]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PCO 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">Solution NMR</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=OH:HYDROXIDE+ION'>OH</scene></td></tr>
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{{STRUCTURE_1pco| PDB=1pco | 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=1pco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pco OCA], [https://pdbe.org/1pco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pco RCSB], [https://www.ebi.ac.uk/pdbsum/1pco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pco ProSAT]</span></td></tr>
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</table>
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===SOLUTION STRUCTURE OF PORCINE PANCREATIC PROCOLIPASE AS DETERMINED FROM 1H HOMONUCLEAR TWO-AND THREE-DIMENSIONAL NMR===
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== Function ==
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[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.
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== Evolutionary Conservation ==
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<!--
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[[Image:Consurf_key_small.gif|200px|right]]
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The line below this paragraph, {{ABSTRACT_PUBMED_7867624}}, adds the Publication Abstract to the page
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Check<jmol>
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(as it appears on PubMed at http://www.pubmed.gov), where 7867624 is the PubMed ID number.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pc/1pco_consurf.spt"</scriptWhenChecked>
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{{ABSTRACT_PUBMED_7867624}}
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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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==About this Structure==
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</jmolCheckbox>
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1PCO is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCO OCA].
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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=1pco ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:7867624</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Boelens, R.]]
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[[Category: Boelens R]]
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[[Category: Breg, J N.]]
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[[Category: Breg JN]]
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[[Category: Cozzone, P J.]]
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[[Category: Cozzone PJ]]
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[[Category: Kaptein, R.]]
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[[Category: Kaptein R]]
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[[Category: Rugani, N.]]
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[[Category: Rugani N]]
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[[Category: Sarda, L.]]
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[[Category: Sarda L]]
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[[Category: Lipase protein cofactor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 16:09:15 2009''
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Current revision

SOLUTION STRUCTURE OF PORCINE PANCREATIC PROCOLIPASE AS DETERMINED FROM 1H HOMONUCLEAR TWO-AND THREE-DIMENSIONAL NMR

PDB ID 1pco

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