Structural and functional studies of legumain-mycocypin complexes revealed a competitive, exosite-regulated mode of interaction.

ABSTRACT: Under pathophysiologic conditions such as Alzheimer's disease and cancer, the endolysosomal cysteine protease legumain was found to translocate to the cytosol, the nucleus, and the extracellular space. These noncanonical localizations demand for a tight regulation of legumain activity, which is in part conferred by protein inhibitors. While there is a significant body of knowledge on the interaction of human legumain with endogenous cystatins, only little is known on its regulation by fungal mycocypins. Mycocypins are characterized by (i) versatile, plastic surface loops allowing them to inhibit different classes of enzymes and (ii) a high resistance toward extremes of pH and temperature. These properties make mycocypins attractive starting points for biotechnological and medical applicati

SUBMITTER: Elamin T 

PROVIDER: S-EPMC9579014 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature