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Dolenc, Iztok; Štefe, Ivica; Turk, Dušan; Taler-Verčič, Ajda; Turk, Boris; Turk, Vito; Stoka, Veronika
Biochimica et biophysica acta. Proteins and proteomics, February 2021, 2021-02-00, 20210201, Volume: 1869, Issue: 2Journal Article
Human cathepsin X belongs to the cathepsin family of 11 lysosomal cysteine proteases. We expressed recombinant procathepsin X in Pichia pastoris in vitro and cleaved it into its active mature form using aspartic cathepsin E. We found, using size exclusion chromatography, X-ray crystallography, and small-angle X-ray scattering, that cathepsin X is a biologically active homodimer with a molecular weight of ~53 kDa. The novel finding that cathepsin X is a dimeric protein opens new horizons in the understanding of its function and the underlying pathophysiological mechanisms of various diseases including neurodegenerative disorders in humans. Display omitted •Procathepsin X is activated by cathepsin E into mature form.•Cathepsin X exists as homodimer of Mw of ~53 kDa.•Both cathepsin X molecules exhibit an extensive binding surface.
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