|PROSITE documentation PDOC00111|
Colipase [1,2,3] is a protein that functions as a cofactor for pancreatic lipase, with which it forms a stoichiometric complex. It also binds to the bile-salt covered triacylglycerol interface thus allowing the enzyme to anchor itself to the water-lipid interface.
As shown in the following schematic representation, colipase is a small protein of approximately 100 amino-acid residues with five conserved disulfide bonds.
+--------+ +--|--+ | +----------+ | | | | | ***** | xxxxxxxxCxxCxCCxxxxxCxxxxCxxxxxCxCxxCxxxxxxxxCxxxx | | | | +-----------------+ +-----------+
'C': conserved cysteine involved in a disulfide bond. '*': position of the pattern.
As a signature pattern for this family, we chose a region which includes two of the cysteines involved in disulfide bonds, as well as three tyrosine residues which seem to be involved in the interfacial binding. We also developed a profile that covers the whole colipase.Last update:
December 2007 / Text revised; profile added.
PROSITE methods (with tools and information) covered by this documentation:
|Title||Pancreatic colipase. Structural and physiological aspects.|
|Source||Biochim. Biophys. Acta 1125:1-7(1992).|
|2||Authors||Chapus C., Rovery M., Sarda L., Verger R.|
|Title||Minireview on pancreatic lipase and colipase.|
|3||Authors||van Tilbeurgh H., Sarda L., Verger R., Cambillau C.|
|Title||Structure of the pancreatic lipase-procolipase complex.|