biostudies-literatureUnknown8(7)Gaboriaud CMannan-binding lectin (MBL), ficolins and collectin-11 are known to associate with three homologous modular proteases, the MBL-Associated Serine Proteases (MASPs). The crystal structures of the catalytic domains of MASP-1 and MASP-2 have been solved, but the structure of the corresponding domain of MASP-3 remains unknown. A link between mutations in the MASP1/3 gene and the rare autosomal recessive 3MC (Mingarelli, Malpuech, Michels and Carnevale,) syndrome, characterized by various developmental disorders, was discovered recently, revealing an unexpected important role of MASP-3 in early developmental processes. To gain a first insight into the enzymatic and structural properties of MASP-3, a recombinant form of its serine protease (SP) domain was produced and characterized. The amidolytiPloS onee67962https://www.ebi.ac.uk/biostudies/studies/S-EPMC3701661biostudies-literatureThe serine protease domain of MASP-3: enzymatic properties and crystal structure in complex with ecotin.PMC3701661Gupta RKRossi VGaboriaud CMartin LLacroix MSerre LArlaud GJThielens NMTeillet FfalseThe serine protease domain of MASP-3: enzymatic properties and crystal structure in complex with ecotin.Mannan-binding lectin (MBL), ficolins and collectin-11 are known to associate with three homologous modular proteases, the MBL-Associated Serine Proteases (MASPs). The crystal structures of the catalytic domains of MASP-1 and MASP-2 have been solved, but the structure of the corresponding domain of MASP-3 remains unknown. A link between mutations in the MASP1/3 gene and the rare autosomal recessive 3MC (Mingarelli, Malpuech, Michels and Carnevale,) syndrome, characterized by various developmental disorders, was discovered recently, revealing an unexpected important role of MASP-3 in early developmental processes. To gain a first insight into the enzymatic and structural properties of MASP-3, a recombinant form of its serine protease (SP) domain was produced and characterized. The amidolyti2013-01-01T00:00:00Z20132026-05-30T02:20:35.756Z2026-05-18T03:07:27.727ZS-EPMC37016612386184010.1371/journal.pone.0067962