Peptidyl-Ser-tetrahedral-intermediate (with previous peptide)
A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis.
Definition and redesign of the extended substrate specificity of granzyme B.
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 21-247.
Crystal structure of the caspase activator human granzyme B, a proteinase highly specific for an Asp-P1 residue.
The structure of the pro-apoptotic protease granzyme B reveals the molecular determinants of its specificity.
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-247.
The three-dimensional structure of human granzyme B compared to caspase-3, key mediators of cell death with cleavage specificity for aspartic acid in P1.
Serine protease mechanism and specificity.
Mechanisms of granule-dependent killing.
Analysis of protein processing by N-terminal proteomics reveals novel species-specific substrate determinants of granzyme B orthologs.
Cytotoxic and non-cytotoxic roles of the CTL/NK protease granzyme B.
Granzyme B-induced apoptosis in cancer cells and its regulation (review).
This enzyme belongs to peptidase family-S1. This enzyme seems to activate caspases, and is involved in apoptosis in cancer cells (see [7], [9], [10]). Since this enzyme has got the same catalytic site as trypsin, it must catalyze the trypsin-like reaction.