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1n8s

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(New page: 200px<br /> <applet load="1n8s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n8s, resolution 3.04&Aring;" /> '''Structure of the pa...)
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[[Image:1n8s.gif|left|200px]]<br />
 
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<applet load="1n8s" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1n8s, resolution 3.04&Aring;" />
 
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'''Structure of the pancreatic lipase-colipase complex'''<br />
 
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==Overview==
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==Structure of the pancreatic lipase-colipase complex==
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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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<StructureSection load='1n8s' size='340' side='right'caption='[[1n8s]], [[Resolution|resolution]] 3.04&Aring;' scene=''>
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== Structural highlights ==
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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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</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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<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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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIPP_HUMAN LIPP_HUMAN]
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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/initialview01.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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==Disease==
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==See Also==
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Known disease associated with this structure: Pancreatic lipase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=246600 246600]]
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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__TOC__
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==About this Structure==
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</StructureSection>
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1N8S is a [http://en.wikipedia.org/wiki/Protein_complex 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]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N8S OCA].
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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: pancreas]]
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[[Category: signal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:19:15 2007''
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Current revision

Structure of the pancreatic lipase-colipase complex

PDB ID 1n8s

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