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1n8s

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Revision as of 08:56, 21 April 2021

Structure of the pancreatic lipase-colipase complex

Structural highlights

1n8s is a 2 chain structure with sequence from Human and Pig. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1lpa, 1lpb
Activity:	Triacylglycerol lipase, with EC number 3.1.1.3
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.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ van Tilbeurgh H, Sarda L, Verger R, Cambillau C. Structure of the pancreatic lipase-procolipase complex. Nature. 1992 Sep 10;359(6391):159-62. PMID:1522902 doi:http://dx.doi.org/10.1038/359159a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n8s"

@@ Line 3: / Line 3: @@
 <StructureSection load='1n8s' size='340' side='right'caption='[[1n8s]], [[Resolution|resolution]] 3.04&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1n8s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Pig Pig]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N8S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1n8s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Pig Pig]. 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>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lpa|1lpa]], [[1lpb|1lpb]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lpa|1lpa]], [[1lpb|1lpb]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1n8s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n8s RCSB], [http://www.ebi.ac.uk/pdbsum/1n8s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n8s 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=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>
 </table>
 == Function ==
-[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Lipase|Lipase]]
+*[[Lipase 3D Structures|Lipase 3D Structures]]
 == References ==
 <references/>

1n8s

From Proteopedia

Revision as of 08:56, 21 April 2021

Structure of the pancreatic lipase-colipase complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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