Function
Mannan-binding lectin serine protease (MASP) are proteases associated with mannan-binding lectin (MLB). The lectin pathway of complement is part of the innate immunity. The pathway activation occurs via recognition of pathogens by MBL followed by activation of MASP leading to activation of the complement system[1].
Relevance
MASP-1 and MASP-2 contribute to clot formation and may represent an important link between inflammation and thrombosis. MASP levels may be altered in vascular diseases[2].
Structural highlights
. MASP-1, MASP-2 and MASP-3 are 680, 671 and 709 amino acid long respectively. They show a similar domain structure with A chain containing domains CUB1, EGF, CUB2, CCP1, CCP2 followed by a short link region and B chain which is the catalytic domain. The catalytic domain contains the classic serine protease active triad of serine, histidine and aspartic acid[3], [4].