Folding incompetence of cathepsin L-like cysteine proteases may be compensated by the highly conserved, domain-building N-terminal extension of the proregion.
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.
Schilling
K
K
Institut für Biochemie I, Klinikum der Friedrich-Schiller-Universität, Jena, Germany.
Pietschmann
S
S
Fehn
M
M
Wenz
I
I
Wiederanders
B
B
D056668:Cathepsin L; D002403:Cathepsins; D017124:Conserved Sequence; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004792:Enzyme Precursors / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D008956:Models, Chemical; D016296:Mutagenesis; D017510:Protein Folding; D017434:Protein Structure, Tertiary
D004792:Enzyme Precursors; D002403:Cathepsins; D003546:Cysteine Endopeptidases; C534281:CTSL protein, human; D056668:Cathepsin L