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1pco

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[[Image:1pco.gif|left|200px]]
 
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{{Structure
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==SOLUTION STRUCTURE OF PORCINE PANCREATIC PROCOLIPASE AS DETERMINED FROM 1H HOMONUCLEAR TWO-AND THREE-DIMENSIONAL NMR==
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|PDB= 1pco |SIZE=350|CAPTION= <scene name='initialview01'>1pco</scene>
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<StructureSection load='1pco' size='340' side='right'caption='[[1pco]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=OH:HYDROXIDE ION'>OH</scene>
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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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|ACTIVITY=
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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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|GENE=
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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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}}
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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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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Procolipase is the precursor of colipase, which acts as protein cofactor for the activity of pancreatic lipase. The solution structure of procolipase has been determined by 1H NMR using two- and three-dimensional measurements. The secondary structure determination identified two separate three-stranded beta-sheet regions with concomitant hydrogen bond patterns. The tertiary structure of the protein was determined using 863 non-trivial proton--proton distance constraints, 14 hydrogen bond distance constraints and 55 phi and 25 X1 dihedral constraints. The structure that was obtained from distance geometry and energy refinement contains three highly disordered loops as well as a disordered N- and C-terminal region. The remaining part of the structure is well defined with a root-mean-square deviation (rmsd) relative to the average of 0.09 +/- 0.02 nm for backbone atoms (residues 11-30, 37-50, 57-69, 83-89). The protein comprises two identical domains, each containing a three-strand beta-sheet and two disulfide bonds: a 15-residue region in each domain superimposes with 0.07 nm rmsd, measured on backbone atoms. The solution structure is nearly identical to the crystal structure. It is in agreement with previous NMR data and, in combination with these data, supports the current model of procolipase micelle interaction and the lipase activation by colipase.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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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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1PCO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCO OCA].
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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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==Reference==
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</jmolCheckbox>
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Solution structure of porcine pancreatic procolipase as determined from 1H homonuclear two-dimensional and three-dimensional NMR., Breg JN, Sarda L, Cozzone PJ, Rugani N, Boelens R, Kaptein R, Eur J Biochem. 1995 Feb 1;227(3):663-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7867624 7867624]
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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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[[Category: Single protein]]
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<div style="clear:both"></div>
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__TOC__
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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: OH]]
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[[Category: lipase protein cofactor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:22:41 2008''
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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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