Skip to main content
. Author manuscript; available in PMC: 2011 Jun 21.
Published in final edited form as: Biochemistry. 2006 Nov 7;45(44):13249–13263. doi: 10.1021/bi0611964

Figure 3.

Figure 3

V8 (Endo-Glu C) or trypsin protease digests of (pro)caspases. V8 digest of procaspase-3(D3A) (A) or of wild-type caspase-3 (B). Trypsin digest of procaspase-3(D3A) (C) or of wild-type caspase-3 (D). (E) Trypsin and V8 protease cleavage sites are mapped onto the caspase-3 structure, and the cleavages are summarized in Table 2. The structure was generated using PyMOL (Delano Scientific). The cleavages at K57, R64, and R207 (underlined) are by trypsin, and the cleavages at E98, E106, E173, D190, E248, and D253 (italicized) are by V8 protease. The primes denote residues from the second heterodimer. Results for the loop bundle mutants are provided as Supporting Information and are summarized in Table 2.