1n8s

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spinqualitylabelsall models 1n8s, resolution 3.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of the pancreatic lipase-colipase complex

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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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