ArticleNature communications2022
Cryo-EM structures reveal the activation and substrate recognition mechanism of human enteropeptidase.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 5 citations in OpenAlex.
- Structural insight into the CUB2 domain's role in enteropeptidase-mediated trypsinogen activation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Discovery of a pyridine-piperazine-based small molecule that enhances the activity of peptidase neurolysin.The Journal of pharmacology and experimental therapeutics · 2026Article
- SCO‑792 alleviates HFD‑aggravated chronic pancreatitis by modulating the gut-pancreas axis via the AMPK/ACC and TLR4/NF‑κB signaling pathways.Frontiers in immunology · 2026Article
- Structural basis of TMPRSS11D specificity and autocleavage activation.Nature communications · 2025Article
- Critical Roles of SEA Domains.Advances in experimental medicine and biology · 2025Review
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 from 2.7 to 4.9 Å. The EP heavy chain was observed to clamp the light chain with CUB2 domain for substrate recognition. The EP light chain N-terminus induced a rearrangement of surface-loops from inactive to active conformations, resulting in activated EP. The heavy chain then served as a hinge for light-chain conformational changes to recruit and subsequently cleave substrate. Our study provides structural insights into rearrangements of EP surface-loops and heavy chain dynamics in the EP catalytic cycle, advancing our understanding of EP-associated pancreatitis.
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