Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2048953 | FEBS Letters | 2010 | 7 Pages |
Abstract
FFAR2 (GPR43) is a receptor for short-chain fatty acids (SCFAs), acetate and propionate. In the current study, we investigate the molecular determinants contributing to receptor activation by endogenous ligands. Mutational analysis revealed several important residues located in transmembrane domains (TM) 3, 4, 5, 6, and 7 for acetate binding. Interestingly, mutations that abolished acetate activity, including the mutation in the well-conserved D(E)RY motif, could be rescued by a recently identified synthetic allosteric agonist. These findings provide additional insight into agonist binding and activation which may aid in designing allosteric ligands for targeting receptor function in various diseases.
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Authors
Gayathri Swaminath, Peter Jaeckel, Qi Guo, Mario Cardozo, Jennifer Weiszmann, Richard Lindberg, Yingcai Wang, Ralf Schwandner, Yang Li,