Ontology highlight
ABSTRACT:
SUBMITTER: Jin H
PROVIDER: S-EPMC4394528 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Jin Hanyong H Zhou Zhenhuan Z Wang Dongmei D Guan Shanshan S Han Weiwei W
International journal of molecular sciences 20150318 3
Acylpeptide hydrolases (APHs) catalyze the removal of N-acylated amino acids from blocked peptides. Like other prolyloligopeptidase (POP) family members, APHs are believed to be important targets for drug design. To date, the binding pose of organophosphorus (OP) compounds of APH, as well as the different OP compounds binding and inducing conformational changes in two domains, namely, α/β hydrolase and β-propeller, remain poorly understood. We report a computational study of APH bound to chlorpy ...[more]