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Function
Human GPR40 (hGPR40) is a G-protein coupled receptor that binds free fatty acids to enhance glucose dependent insulin signaling.[3]
Structure
Like most G-protein coupled receptors, hGPR40 contains seven transmembrane helices. In order obtain a crystallized structure of the protein, four (, , , ) were made to increase expression levels and thermal stability of the protein.[3]
Charge Network
hGPR40 has a distinct binding pocket that is established by seven key residues. The importance of these residues for agonist binding was determined by mutagenesis studies. Each of these residues have either a charged or polar R-group that allows them to develop a charge network that interacts with the carboxylate moiety of agonists. In 2007 and 2009 researchers showed the presence of Arg 183 and Arg 258 in the binding pocket [4][5] Along with the two Arginine residues, the charge network incorporates two Tyrosine residues.These residues (Tyr 91 and Tyr 240) also stabilize the carboxylate of the agonists. It was further determined that Tyr 240 is epecially important for binding. Mutation of Tyr 240 caused a reduction in the binding affinity of TAK-875 by eight fold and had a significant effect on the Kd of the protein.[3]
ECl2
Clinical Relevance
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