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Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum Cardoso, R.M.F., Daniels, D.S., Bruns, C.M., Tainer, J.A
The EM structures (Figure 2b) of the receptor revealed that it is composed of: The extracellular domain (E) of the GLP-1 receptor binds the GLP-1 protein A seven transmembrane helical domain (TM1-7) with the -helices separated by three intracellular loops (IC1-3) and three extracellular loops (EC1-3) An intracellular (Cytoplasmic) C-terminus that interacts with G-Protein which is responsible for signaling The extracellular domain: The N-terminal ~120 amino acids of the extracellular domain of the GLP-1R protein has one long and one short helix, two beta strands forming a sheet and several loops joining these secondary structural elements
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Semaglutide medication belongs to a class of medication known as GLP-1 receptor agonists
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