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Biol Chem. 2001 May;382(5):859-65.

Folding incompetence of cathepsin L-like cysteine proteases may be compensated by the highly conserved, domain-building N-terminal extension of the proregion.

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Institut für Biochemie I, Klinikum der Friedrich-Schiller-Universität, Jena, Germany.


Folding of cathepsins L and S depend upon their proregion which extends the enzyme part by about 100 amino acids. Only a minority of the prosequence follows the structural template provided by the enzyme part; the majority forms an autonomous minidomain fairly distant from the active site cleft. We suggest that this prodomain may be the structural correlate of a foldase function of the proregion within the cathepsin L-like subfamily of papain-type cysteine proteases and report on a functional approach supporting this hypothesis.

[Indexed for MEDLINE]

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