Folding incompetence of cathepsin L-like cysteine proteases may be compensated by the highly conserved, domain-building N-terminal extension of the proregion.
Biol Chem
; 382(5): 859-65, 2001 May.
Article
en En
| MEDLINE
| ID: mdl-11517942
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Cisteína Endopeptidasas
/
Pliegue de Proteína
/
Precursores Enzimáticos
/
Modelos Químicos
Límite:
Humans
Idioma:
En
Revista:
Biol Chem
Asunto de la revista:
BIOQUIMICA
Año:
2001
Tipo del documento:
Article
País de afiliación:
Alemania
Pais de publicación:
Alemania