Mannan-binding lectin serine protease
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3D structures of mannan-binding lectin serine protease
Updated on 14-December-2025
FunctionMannan-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]. RelevanceMASP-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 highlightsHuman MASP-2 sushi 2 domain and catalytic domain complex with protease inhibitor SGPI-2. 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].
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Updated on 14-December-2025
This page was last modified 11:02, 14 December 2025.