Folding incompetence of cathepsin L-like cysteine proteases may be compensated by the highly conserved, domain-building N-terminal extension of the proregion
K Schilling, S Pietschmann, M Fehn, I Wenz… - Biological …, 2001 - degruyter.com
K Schilling, S Pietschmann, M Fehn, I Wenz, B Wiederanders
Biological chemistry, 2001•degruyter.comFolding 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.
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.
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.
De Gruyter