1N8S

Structure of the pancreatic lipase-colipase complex

Summary for 1N8S

• Entry DOI: 10.2210/pdb1n8s/pdb
• Related: 1LPA 1LPB
• Descriptor: Triacylglycerol lipase, pancreatic, colipase II (2 entities in total)
• Functional Keywords: hydrolase, pancreas
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted : P16233 P02703
• Total number of polymer chains: 2
• Total formula weight: 59919.29

Authors

van Tilbeurgh, H.,Sarda, L.,Verger, R.,Cambillau, C. (deposition date: 2002-11-21, release date: 2002-12-18, Last modification date: 2024-11-06)

Primary citation

van Tilbeurgh, H.,Sarda, L.,Verger, R.,Cambillau, C.
Structure of the pancreatic lipase-procolipase complex
Nature, 359:159-162, 1992

PubMed Abstract: 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.

PubMed: 1522902
DOI: 10.1038/359159a0

Experimental method

X-RAY DIFFRACTION (3.04 Å)