In this task, you are given an abstract of article. Your task is to generate title for this article. Preferred titles are under thirty words.

The class B glucagon-like peptide-1 (GLP-1) G protein-coupled receptor is a major target for the treatment of type 2 diabetes and obesity. Endogenous and mimetic GLP-1 peptides exhibit biased agonisma difference in functional selectivitythat may provide improved therapeutic outcomes. Here we describe the structure of the human GLP-1 receptor in complex with the G protein-biased peptide exendin-P5 and a Gs heterotrimer, determined at a global resolution of 3.3 A. At the extracellular surface, the organization of extracellular loop 3 and proximal transmembrane segments differs between our exendin-P5-bound structure and previous GLP-1-bound GLP-1 receptor structure. At the intracellular face, there was a six-degree difference in the angle of the Gs5 helix engagement between structures, which was propagated across the G protein heterotrimer. In addition, the structures differed in the rate and extent of conformational reorganization of the Gs protein. Our structure provides insights into the molecular basis of biased agonism.
Phase-plate cryo-EM structure of a biased agonist-bound human GLP-1 receptorGs complex