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Article

Distal mutation V486M disrupts the catalytic activity of DPP4 by affecting the flap of the propeller domain.

Acta pharmacologica Sinica - 1 Aug 2022

Li Teng-Teng, Peng Cheng, Wang Ji-Qiu, Xu Zhi-Jian, Su Ming-Bo, Li Jia, Zhu Wei-Liang, Li Jing-Ya

Abstract excerpt

Dipeptidyl peptidase-4 (DPP4) plays a crucial role in regulating the bioactivity of glucagon-like peptide-1 (GLP-1) that enhances insulin secretion and pancreatic β-cell proliferation, making it a therapeutic target for type 2 diabetes. Although the crystal structure of DPP4 has been determined, its structure-function mechanism is largely unknown. Here, we examined the biochemical properties of sporadic human...

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Identifiers

PMID: 34907358
DOI: 10.1038/s41401-021-00818-x
PMCID: PMC8669218

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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