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. Author manuscript; available in PMC: 2012 Nov 5.
Published in final edited form as: Physiol Rev. 2012 Jul;92(3):1189–1234. doi: 10.1152/physrev.00015.2011

Table 1.

AChR ligand binding site multiloop structure

Loop Residue Span Secondary Structure Key Residues Defining Ligands
A α93-97 β4-β5 linker Tyr93, Ala96, Asp97 Nicotine, ACh
B α148-153 β7-β8 linker Trp149, Tyr151, Gly153 Nicotine, ACh, d-tubocurarine
C α189-200 β9-β10 linker Tyr190, Cys192, Cys193, Tyr198, Asp200 Nicotine, ACh, bromo-ACh, lophotoxin
D ε55-59, δ57-61 β2-strand εTrp55, εGly57, εAsp59, δTrp57, δGlu59, δGly61 d-Tubocurarine, metocurine, nicotine, ACh, NmmI α-toxin, Waglerin I
E ε109-119, δ111-121 β5′-β6-strands εLeu109, εTyr111, εVal116, εThr117, εLeu119, δLeu111, δTyr113, δVal118, δTyr119, δLeu121 α-Conotoxin M1, d-tubocurarine, metocurine, α -bungarotoxin, NmmI α-toxin, Waglerin I
F ε161-183, δ163-187 β8-β9 linker εAsp173, εAsp175, δIle178, δAsp180 α-Conotoxin M1, metocurine, NmmI α-toxin, ACh, Waglerin I
G ε29-45, δ31-47 β1-strand εLys34, δAla36 α-Conotoxin M1, carbamylcholine

Residue positions correspond to the human endplate AChR.