Ontology highlight
ABSTRACT:
SUBMITTER: Thomsen ND
PROVIDER: S-EPMC3666719 | biostudies-literature | 2013 May
REPOSITORIES: biostudies-literature
Thomsen Nathan D ND Koerber James T JT Wells James A JA
Proceedings of the National Academy of Sciences of the United States of America 20130506 21
Procaspase-3 (P3) and procaspase-7 (P7) are activated through proteolytic maturation to form caspase-3 (C3) and caspase-7 (C7), respectively, which serve overlapping but nonredundant roles as the executioners of apoptosis in humans. However, it is unclear if differences in P3 and P7 maturation mechanisms underlie their unique biological functions, as the structure of P3 remains unknown. Here, we report structures of P3 in a catalytically inactive conformation, structures of P3 and P7 bound to co ...[more]