Activities of the MBL-associated serine proteases (MASPs) and their regulation by natural inhibitors |
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| Authors: | Wong N K Kojima M Dobó J Ambrus G Sim R B |
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| Affiliation: | Department of Biochemistry, University of Oxford, UK. |
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| Abstract: | There has been rapid progress in determining the mechanism by which complement is activated by the complex formed between Mannose-Binding Lectin and its associated proteases (MASPs). MBL and the MASPs are of low abundance, but are similar to the more abundant C1q-C1r2s2 complex (C1), which has been extensively investigated. In this review we summarise recent findings on MBL-MASPs' structure. enzymic activity and regulation, and compare MBL-MASPs with C1. |
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