Dominguez_2000_FEBS.Lett_482_109

Reference

Title : Interactions of bile salt micelles and colipase studied through intermolecular nOes - Dominguez_2000_FEBS.Lett_482_109
Author(s) : Dominguez C , Sebban-Kreuzer C , Bornet O , Kerfelec B , Chapus C , Guerlesquin F
Ref : FEBS Letters , 482 :109 , 2000
Abstract :

Colipase is a small protein (10 kDa), which acts as a protein cofactor for the pancreatic lipase. Various models of the activated ternary complex (lipase-colipase-bile salt micelles) have been proposed using detergent micelles, but no structural information has been established with bile salt micelles. We have investigated the organization of sodium taurodeoxycholate (NaTDC) micelles and their interactions with pig and horse colipases by homonuclear nuclear magnetic resonance (NMR) spectroscopy. The NMR data supply evidence that the folding of horse colipase is similar to that already described for pig colipase. Intermolecular nuclear Overhauser effects have shown that two conserved aromatic residues interact with NaTDC micelles.

PubMedSearch : Dominguez_2000_FEBS.Lett_482_109
PubMedID: 11018532

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Citations formats

Dominguez C, Sebban-Kreuzer C, Bornet O, Kerfelec B, Chapus C, Guerlesquin F (2000)
Interactions of bile salt micelles and colipase studied through intermolecular nOes
FEBS Letters 482 :109

Dominguez C, Sebban-Kreuzer C, Bornet O, Kerfelec B, Chapus C, Guerlesquin F (2000)
FEBS Letters 482 :109