The C3 protein is the central molecule within the complement system and undergoes proteolytic activation to C3b in the presence of pathogens. Pattern-independent activation of C3 also occurs via hydrolysis, resulting in C3(HO), but the structural details of C3 hydrolysis remain elusive. Here we show that the conformation of the C3(HO) analog, C3MA, is indistinguishable from C3b.
View Article and Find Full Text PDFThe ability to regulate transmembrane ion transport in response to various cues is vital to any living cell. In neurons, one key example of critical ion control relates to the extrusion of chloride mediated by the potassium-chloride-cotransporters (KCC1-4). In a recent hallmark study, Chi et␣al (2021) report cryo-EM structures of human KCC1 and KCC3b, delineating in detail how regulation by phosphorylation inhibits the transport activity.
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