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Accueil > Publications > Recherche par années > Années 1990 > 1998

Roussel, A ; de Caro, J ; Bezzine, S ; Gastinel, L ; de Caro, A ; Carriere, F ; Leydier, S ; Verger, R ; Cambillau, C

Reactivation of the totally inactive pancreatic lipase RP1 by structure-predicted point mutations

Proteins-Structure Function and Genetics 32 (4) 523-531

par Administrateur - publié le

Abstract :

Both classical pancreatic lipase (DPL) and pancreatic lipase-related protein 1 (DPLRP1) have been found to be secreted by dog exocrine pancreas. These two proteins were purified to homogeneity from canine pancreatic juice and no significant catalytic activity was observed with dog PLRP1 on any of the substrates tested : di- and tri-glycerides, phospholipids, etc. DPLRP1 was crystallized and its structure solved by molecular replacement and refined at a resolution of 2.10 Angstrom Its structure is similar to that of the classical PL structures in the absence of any inhibitors or micelles, The lid domain that controls the access to the active site was found to have a closed conformation.