Foldase function of the cathepsin S proregion is strictly based upon its domain structure.
Folding of cathepsin S, like other cathepsin L-like proteases, depends on its proregion. The major part of the proregion forms a small domain distal from the catalytic centre, suggesting function(s) beyond active-site shielding. Using an optimised in vitro trans-refolding assay, we compared reactivation of denatured cathepsin S by the genuine propeptide, wild-type 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.
Pietschmann
Sandra
S
Institut für Biochemie I, Klinikum der Friedrich-Schiller-Universität, Jena, Germany.
Fehn
Marc
M
Kaulmann
Guido
G
Wenz
Ingrid
I
Wiederanders
Bernd
B
Schilling
Klaus
K
D000595:Amino Acid Sequence; D002403:Cathepsins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004792:Enzyme Precursors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D004792:Enzyme Precursors; D002403:Cathepsins; C028217:cathepsin S