IndraLab
Statements
sparser
"AZ1, VSM, and FT206 bind to USP28 at different overlapping positions inside the same hydrophobic cleft, located at the intersection of the USP-thumb and palm subdomains in the center of the concave part of the USP S1-site, which acts as a binding surface for the globular domain of the distal Ub moiety of the cleaved substrate (Figs. xref and xref )."
sparser
"However, the observation that the three structurally and chemically different compounds AZ1, VSM, and FT206 interact with USP28 in the same cleft, yet exert their inhibitory activity for USP28 and its close homolog USP25 without significantly affecting other DUBs of the USP family, prompted us to further investigate the origin of this selectivity."