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Article

The dimeric transmembrane domain of prolyl dipeptidase DPP-IV contributes to its quaternary structure and enzymatic activities.

Protein science : a publication of the Protein Society - 1 Sept 2010

Chung Kuei-Min, Cheng Jai-Hong, Suen Ching-Shu, Huang Chih-Hsiang, Tsai Cheng-Han, Huang Li-Hao, Chen Yi-Rong, Wang Andrew H-J, Jiaang Weir-Torn, Hwang Ming-Jing, Chen Xin

Abstract excerpt

Dipeptidyl peptidase IV (DPP-IV) is a drug target in the treatment of human type II diabetes. It is a type II membrane protein with a single transmembrane domain (TMD) anchoring the extracellular catalytic domain to the membrane. DPP-IV is active as a dimer, with two dimer interacting surfaces located extracellularly. In this study, we demonstrate that the TM of DPP-IV promotes DPP-IV dimerization and rescues...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 20572019
DOI: 10.1002/pro.443
PMCID: PMC2975127

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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