PROSITE documentation PDOC00111

Colipase family signature and profile





Description

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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

COLIPASE_2, PS51342; Colipase family profile  (MATRIX)

COLIPASE_1, PS00121; Colipase signature  (PATTERN)


References

1AuthorsErlanson-Albertsson C.
TitlePancreatic colipase. Structural and physiological aspects.
SourceBiochim. Biophys. Acta 1125:1-7(1992).
PubMed ID1567900

2AuthorsChapus C., Rovery M., Sarda L., Verger R.
TitleMinireview on pancreatic lipase and colipase.
SourceBiochimie 70:1223-1234(1988).
PubMed ID3147715

3Authorsvan Tilbeurgh H., Sarda L., Verger R., Cambillau C.
TitleStructure of the pancreatic lipase-procolipase complex.
SourceNature 359:159-162(1992).
PubMed ID1522902
DOI10.1038/359159a0



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