{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8(7)"],"submitter":["Gaboriaud C"],"pubmed_abstract":["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 amidolyti"],"journal":["PloS one"],"pagination":["e67962"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3701661"],"repository":["biostudies-literature"],"pubmed_title":["The serine protease domain of MASP-3: enzymatic properties and crystal structure in complex with ecotin."],"pmcid":["PMC3701661"],"pubmed_authors":["Gupta RK","Rossi V","Gaboriaud C","Martin L","Lacroix M","Serre L","Arlaud GJ","Thielens NM","Teillet F"],"additional_accession":[]},"is_claimable":false,"name":"The serine protease domain of MASP-3: enzymatic properties and crystal structure in complex with ecotin.","description":"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 amidolyti","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013","modification":"2026-05-30T02:20:35.756Z","creation":"2026-05-18T03:07:27.727Z"},"accession":"S-EPMC3701661","cross_references":{"pubmed":["23861840"],"doi":["10.1371/journal.pone.0067962"]}}