Ontology highlight
ABSTRACT:
SUBMITTER: Yang X
PROVIDER: S-EPMC9663175 | biostudies-literature | 2022 Nov
REPOSITORIES: biostudies-literature
Yang Xiaoli X Ding Zhanyu Z Peng Lisi L Song Qiuyue Q Zhang Deyu D Cui Fang F Cui Fang F Xia Chuanchao C Li Keliang K Yin Hua H Li Shiyu S Li Zhaoshen Z Huang Haojie H
Nature communications 20221114 1
Enteropeptidase (EP) initiates intestinal digestion by proteolytically processing trypsinogen, generating catalytically active trypsin. EP dysfunction causes a series of pancreatic diseases including acute necrotizing pancreatitis. However, the molecular mechanisms of EP activation and substrate recognition remain elusive, due to the lack of structural information on the EP heavy chain. Here, we report cryo-EM structures of human EP in inactive, active, and substrate-bound states at resolutions ...[more]