1n8s
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Interfacial adsorption of pancreatic lipase is strongly dependent on the | + | 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. |
==Disease== | ==Disease== | ||
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[[Category: Cambillau, C.]] | [[Category: Cambillau, C.]] | ||
[[Category: Sarda, L.]] | [[Category: Sarda, L.]] | ||
| - | [[Category: Tilbeurgh, H | + | [[Category: Tilbeurgh, H van.]] |
[[Category: Verger, R.]] | [[Category: Verger, R.]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: signal]] | [[Category: signal]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:26 2008'' |
Revision as of 12:03, 21 February 2008
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Structure of the pancreatic lipase-colipase complex
Contents |
Overview
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.
Disease
Known disease associated with this structure: Pancreatic lipase deficiency OMIM:[246600]
About this Structure
1N8S is a Protein complex structure of sequences from Homo sapiens and Sus scrofa. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.
Reference
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
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