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Dimerization/oligomerization of the extracellular domain of the GLP-1 receptor and the negative cooperativity in its ligand binding revealed by the improved NanoBiT

FASEB J. 2020; 
Song X, Yu Y, Shen C, Wang Y, Wang N.
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Recombinant Proteins … composition unknown Exenatide and imidazole were from Meilun Biotech (Dalian, China) GLP-1 (7-36) was from GenScript Biotech (Nanjing, China) Dulaglutide was a kind gift from Professor Zhufang Shen of this Institute Oxidized … Get A Quote

摘要

The glucagon-like peptide-1 receptor (GLP-1R), a family B G-protein coupled receptor (GPCR), regulates the insulin secretion following stimulation by ligands. The transmembrane domain (TM) mediates GLP-1R homodimerization, which modulates its ligand binding and signaling. We investigated the possible involvement of the N-terminal extracellular domain (NTD) in dimerization/oligomerization and dimer-associated ligand binding by NanoLuc Binary Technology (NanoBiT). With improved NanoBiT detection using a decreasing substrate concentration, the negative cooperativity of ligand binding to the NTD was confirmed by accelerated dissociation and Scatchard analysis. The dimerization/oligomerization of the isolated NTD wa... More

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