1n8s

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[[Image:1n8s.jpg|left|200px]]
 
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{{Structure
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==Structure of the pancreatic lipase-colipase complex==
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|PDB= 1n8s |SIZE=350|CAPTION= <scene name='initialview01'>1n8s</scene>, resolution 3.04&Aring;
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<StructureSection load='1n8s' size='340' side='right'caption='[[1n8s]], [[Resolution|resolution]] 3.04&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1n8s]] 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=1N8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N8S FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span>
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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]] 3.04&#8491;</td></tr>
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|GENE=
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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=1n8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8s OCA], [https://pdbe.org/1n8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n8s RCSB], [https://www.ebi.ac.uk/pdbsum/1n8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n8s ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1lpa|1LPA]], [[1lpb|1LPB]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8s OCA], [http://www.ebi.ac.uk/pdbsum/1n8s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n8s RCSB]</span>
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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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}}
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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/n8/1n8s_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1n8s ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Interfacial adsorption of pancreatic lipase is strongly dependent on the physical chemical properties of the lipid surface. These properties are affected by amphiphiles such as phospholipids and bile salts. In the presence of such amphiphiles, lipase binding to the interface requires a protein cofactor, colipase. We obtained crystals of the pancreatic lipase-procolipase complex and solved the structure at 3.04 A resolution. Here we describe the structure of procolipase, which essentially consists of three 'fingers' and is topologically comparable to snake toxins. The tips of the fingers contain most of the hydrophobic amino acids and presumably form the interfacial binding site. Lipase binding occurs at the opposite side to this site and involves polar interactions. Determination of the three-dimensional structure of pancreatic lipase has revealed the presence of two domains: an amino-terminal domain, at residues 1-336 containing the active site and a carboxy-terminal domain at residues 337-449 (ref. 6). Procolipase binds exclusively to the C-terminal domain of lipase. No conformational change in the lipase molecule is induced by the binding of procolipase.
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'''Structure of the pancreatic lipase-colipase complex'''
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Structure of the pancreatic lipase-procolipase complex.,van Tilbeurgh H, Sarda L, Verger R, Cambillau C Nature. 1992 Sep 10;359(6391):159-62. PMID:1522902<ref>PMID:1522902</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1n8s" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Interfacial adsorption of pancreatic lipase is strongly dependent on the physical chemical properties of the lipid surface. These properties are affected by amphiphiles such as phospholipids and bile salts. In the presence of such amphiphiles, lipase binding to the interface requires a protein cofactor, colipase. We obtained crystals of the pancreatic lipase-procolipase complex and solved the structure at 3.04 A resolution. Here we describe the structure of procolipase, which essentially consists of three 'fingers' and is topologically comparable to snake toxins. The tips of the fingers contain most of the hydrophobic amino acids and presumably form the interfacial binding site. Lipase binding occurs at the opposite side to this site and involves polar interactions. Determination of the three-dimensional structure of pancreatic lipase has revealed the presence of two domains: an amino-terminal domain, at residues 1-336 containing the active site and a carboxy-terminal domain at residues 337-449 (ref. 6). Procolipase binds exclusively to the C-terminal domain of lipase. No conformational change in the lipase molecule is induced by the binding of procolipase.
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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== References ==
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==About this Structure==
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<references/>
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1N8S is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8S OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Structure of the pancreatic lipase-procolipase complex., van Tilbeurgh H, Sarda L, Verger R, Cambillau C, Nature. 1992 Sep 10;359(6391):159-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1522902 1522902]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Cambillau C]]
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[[Category: Cambillau, C.]]
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[[Category: Sarda L]]
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[[Category: Sarda, L.]]
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[[Category: Verger R]]
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[[Category: Tilbeurgh, H van.]]
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[[Category: Van Tilbeurgh H]]
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[[Category: Verger, R.]]
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[[Category: hydrolase]]
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[[Category: pancrea]]
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[[Category: signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:27:06 2008''
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Current revision

Structure of the pancreatic lipase-colipase complex

PDB ID 1n8s

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