title: Assembly of C1 and the MBL- and ficolin-MASP complexes: structural insights.
abstract: The classical pathway C1 complex, and the MBL-MASP and ficolin-MASP complexes involved in activation of the lectin pathway have several features in common. Both types of complexes are assembled from two subunits: an oligomeric recognition protein (C1q, MBL, L-, H- or M-ficolin), and a protease component, which is either a tetramer (C1s-C1r-C1r-C1s) or a dimer ((MASP)(2)). Recent functional and 3-D structural investigations have revealed that C1r/C1s and the MASPs associate through a common mechanism involving their N-terminal CUB1-EGF region. In contrast, the C1s-C1r-C1r-C1s tetramer and the (MASP)(2) dimers appear to have evolved distinct strategies to associate with their partner proteins. The purpose of this article is to review these recent advances.
authors.affiliation: Laboratoire de Cristallographie et Cristallogénèse des Protéines, France.
authors.forename: Christine
authors.initials: C
authors.lastname: Gaboriaud
authors.forename: Florence
authors.initials: F
authors.lastname: Teillet
authors.forename: Lynn A
authors.initials: LA
authors.lastname: Gregory
authors.forename: Nicole M
authors.initials: NM
authors.lastname: Thielens
authors.forename: Gérard J
authors.initials: GJ
authors.lastname: Arlaud
mesh_terms: D000818:Animals; D003172:Complement C1 / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D037601:Mannose-Binding Lectin / Q000737:chemistry / Q000378:metabolism*; D050606:Mannose-Binding Protein-Associated Serine Proteases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D000097604:Ficolins
chemical_list: D003172:Complement C1; D037102:Lectins; D037601:Mannose-Binding Lectin; D050606:Mannose-Binding Protein-Associated Serine Proteases; D000097604:Ficolins