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==SOLUTION STRUCTURE OF PORCINE PANCREATIC PROCOLIPASE AS DETERMINED FROM 1H HOMONUCLEAR TWO-AND THREE-DIMENSIONAL NMR==
==SOLUTION STRUCTURE OF PORCINE PANCREATIC PROCOLIPASE AS DETERMINED FROM 1H HOMONUCLEAR TWO-AND THREE-DIMENSIONAL NMR==
<StructureSection load='1pcn' size='340' side='right'caption='[[1pcn]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1pcn' size='340' side='right'caption='[[1pcn]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1pcn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PCN FirstGlance]. <br>
<table><tr><td colspan='2'>[[1pcn]] 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=1PCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PCN FirstGlance]. <br>
</td></tr><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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pco|1pco]]</div></td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pcn OCA], [https://pdbe.org/1pcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pcn RCSB], [https://www.ebi.ac.uk/pdbsum/1pcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pcn ProSAT]</span></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=1pcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pcn OCA], [https://pdbe.org/1pcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pcn RCSB], [https://www.ebi.ac.uk/pdbsum/1pcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pcn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1pcn ConSurf].
</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=1pcn ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:7867624<ref>PMID:7867624</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pcn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pig]]
[[Category: Sus scrofa]]
[[Category: Boelens, R]]
[[Category: Boelens R]]
[[Category: Breg, J N]]
[[Category: Breg JN]]
[[Category: Cozzone, P J]]
[[Category: Cozzone PJ]]
[[Category: Kaptein, R]]
[[Category: Kaptein R]]
[[Category: Rugani, N]]
[[Category: Rugani N]]
[[Category: Sarda, L]]
[[Category: Sarda L]]
[[Category: Lipase protein cofactor]]

Revision as of 08:54, 17 April 2024

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

Structural highlights

1pcn is a 1 chain structure with sequence from Sus scrofa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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