Extracellular loop 2 of g protein-coupled olfactory receptors is critical for odorant recognition

HIGHLIGHTS

• who: Yiqun Yu from the in ECL2, R I, N D, L V, and L M (Fig A). These residues flank the ECL2-, disulfide bond, suggesting that this region (residues, ) is important for the receptor function. Five residues in this region are conserved in mOR256, and mOR256, (H176, , and, ). Therefore, we mutated these five residues in m, to evaluate their role in this promiscuous receptor. They were mutated into alanine, except for, which was mutated into a bulky isoleucine. While F A impaired receptor expression on the cell surface (Fig., ), the other four mutations systematically diminished the . . .
  

   

  

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