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Updated: Sep 5, 2026

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
Published on: March 18, 2010
C1s, the protease messenger of C1. Structure, function and physiological significance
Péter Gál1, Géza Ambrus, Péter Závodszky
1Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest.
Abstract:
C1s is the modular serine protease, which executes the catalytic function of the C1 complex: the cleavage of C4 and C2. Like other complement serine proteases C1s has restricted substrate specificity and it is engaged into specific interactions with other subcomponents of the complement system. There has been a rapid progress in determining the 3D structure of complement serine proteases and in revealing the role of the individual domains in the protein-protein interaction properties. In this review we summarize recent findings on the structure of C1s, and on the mechanism of action of this protease. The results obtained by genetic engineering, physico-chemical and functional studies are reviewed. The physiological relevance of the proteolytic action of C1s and its possible implications in health and disease will also be discussed.
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