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.