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. 2019 Mar 5;42(5):426–435. doi: 10.1007/s12272-019-01134-z

Fig. 1.

Fig. 1

α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) structure and palmitoylation. Schematic diagrams show each of the four AMPAR subunits. In each diagram, the large extracellular N-terminal domain includes S1, which forms the glutamate binding site together with S2 that is located on the extracellular loop linking transmembrane domain 3 (TMD3) and TMD4. Four hydrophobic TMDs including three membrane-spanning TMDs (TMD1, TMD3, and TMD4) and one membrane-embedded TMD (TMD2) and three intracellular domains (intracellular loop1, loop2, and the cytoplasmic tail) are shown. Palmitoylation sites for each subunit are marked in red