Journal
MOLECULAR IMMUNOLOGY
Volume 46, Issue 14, Pages 2745-2752Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2009.04.026
Keywords
Complement system; Serine protease; 3D structure; Substrate specificity; Autoactivation
Categories
Ask authors/readers for more resources
C1r, C1s and the mannose-binding lectin-associated serine proteases (MASPs) are responsible for the initiation of the classical- and lectin pathway activation of the complement system. These enzymes do not act alone, but form supramolecular complexes with pattern recognition molecules such as C1q, MBL, and ficolins. They share the same domain organization but have different substrate specificities and fulfill different physiological functions. In the recent years the rapid progress of structural biology facilitated the understanding of the molecular mechanism of complement activation at atomic level. In this review we summarize our current knowledge about the structure and function of the early complement proteases, delineate the latest models of the multimolecular complexes and present the functional consequences inferred from the structural studies. We also discuss some open questions and debated issues that need to be resolved in the future. (C) 2009 Elsevier Ltd. All rights reserved
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available