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Biochim Biophys Acta. 1999 Nov 23;1441(2-3):173-84.

Colipase: structure and interaction with pancreatic lipase.

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  • 1Architecture et Fonction des Macromol√©cules Biologiques, CNRS-IFR1 UPR9039, GBMA, 163 Avenue de Luminy Case 925, 13288, Marseille, France.vantil@esil.univ-mrs.fr

Abstract

Colipase is a small protein cofactor needed by pancreatic lipase for the efficient dietary lipid hydrolysis. It binds to the C-terminal, non-catalytic domain of lipase, thereby stabilising an active conformation and considerably increasing the overall hydrophobic binding site. Structural studies of the complex and of colipase alone have clearly revealed the functionality of its architecture. Interestingly, a structural analogy has recently been discovered between colipase and a domain in a developmental protein (Dickkopf), based on sequence analogy and homology modeling. Whether this structural analogy implies a common function (lipid interaction) remains to be clarified. Structural analogies have also been recognised between the pancreatic lipase C-terminal domain, the N-terminal domains of lipoxygenases and the C-terminal domain of alpha-toxin. These non-catalytic domains in the latter enzymes are important for interaction with membranes. It has not been established if these domains are also involved in eventual protein cofactor binding as is the case for pancreatic lipase.

PMID:
10570245
[PubMed - indexed for MEDLINE]
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