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Licensed Unlicensed Requires Authentication Published by De Gruyter June 1, 2005

Foldase Function of the Cathepsin S Proregion Is Strictly Based upon Its Domain Structure

  • S. Pietschmann , M. Fehn , G. Kaulmann , B. Wiederanders I. Wenz and K. Schilling
From the journal Biological Chemistry


Folding of cathepsin S, like other cathepsin Llike proteases, depends on its proregion. The major part of the proregion forms a small domain distal from the catalytic centre, suggesting function(s) beyond activesite shielding. Using an optimised in vitro transrefolding assay, we compared reactivation of denatured cathepsin S by the genuine propeptide, wildtype and ten selected mutants. Including structural data and binding constants, we identified the prodomain core and the hairpin region to be important for the foldase function.

Published Online: 2005-06-01
Published in Print: 2002-09-17

Copyright © 2002 by Walter de Gruyter GmbH & Co. KG

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