Figure 1.
Figure 1. AChR and AChBP structures. (A) Torpedo AChR α and δ subunits (Protein Data Bank accession no. 2bg9; Unwin, 2005). ECD, extracellular domain; TMD, transmembrane domain. Horizontal lines mark approximately the membrane. Purple, loop C; blue,β9–10; green, ECD–TMD interface; tan, αM2. Spheres, on-pathway residues (gray) αW149 (binding site), αP272 (M2–M3 linker), and αL251 (M2-9’ gate region), and off-pathway residues (white) δP123 (loop D; aligns with εP121) and αA96 (loop A) (see Fig. 4). (B) Close-up view of the Lymnaea stagnalis AChBP ligand-binding site (Protein Data Bank accession no. 1uv6; Celie et al., 2004). White, primary subunit (α in AChRs); tan, complementary subunit (ε or δ in AChRs); green, the four core aromatic residues (AChR numbering); ligand, carbamylcholine. Spheres, αC atoms of the terminal residues of loop C (αV188 and αY198 in mouse AChRs).

AChR and AChBP structures. (A) Torpedo AChR α and δ subunits (Protein Data Bank accession no. 2bg9; Unwin, 2005). ECD, extracellular domain; TMD, transmembrane domain. Horizontal lines mark approximately the membrane. Purple, loop C; blue,β9–10; green, ECD–TMD interface; tan, αM2. Spheres, on-pathway residues (gray) αW149 (binding site), αP272 (M2–M3 linker), and αL251 (M2-9’ gate region), and off-pathway residues (white) δP123 (loop D; aligns with εP121) and αA96 (loop A) (see Fig. 4). (B) Close-up view of the Lymnaea stagnalis AChBP ligand-binding site (Protein Data Bank accession no. 1uv6; Celie et al., 2004). White, primary subunit (α in AChRs); tan, complementary subunit (ε or δ in AChRs); green, the four core aromatic residues (AChR numbering); ligand, carbamylcholine. Spheres, αC atoms of the terminal residues of loop C (αV188 and αY198 in mouse AChRs).

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