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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
https://doi.org/10.1515/BC.2002.165

Abstract

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.

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

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

From the journal
Biological Chemistry
Biological Chemistry
Volume 383 Issue 9
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