 |
|
Title
|
|
Structure of the pancreatic lipase-procolipase complex.
|
|
|
Authors
|
|
H.van Tilbeurgh,
L.Sarda,
R.Verger,
C.Cambillau.
|
|
|
Ref.
|
|
Nature, 1992,
359,
159-162.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|