Fig. 1: C4-α7 cryo-EM structures in the absence or presence of nicotine. | Nature Communications

Fig. 1: C4-α7 cryo-EM structures in the absence or presence of nicotine.

From: An original potentiating mechanism revealed by the cryo-EM structures of the human α7 nicotinic receptor in complex with nanobodies

Fig. 1

a Unsharpened maps of the α7∆ICDcryo in complex with C4 (C4-Apo, left) and of the α7FLcryo in complex with C4 and nicotine (C4-Nic, right) with densities contoured at 2σ. The dashed boxes denote the parts that were used for model building. b Top and side views of the C4-Apo structure, protein chains are depicted in white (α7 apo-) and purple (C4). The structure is shown exploded in (c). c Top: Bottom view of the ring of C4 with the molecular surface of the three CDRs colored in shades of purple. Bottom: Top view of the ECD of α7 with N-ter helices, MIR and pre-β1 colored in yellow, pink and green, respectively. The groove in which the CDRs are plunging is delimited with a dashed line. d Side view of the C4-Apo structure, represented in cartoon with α7 in white and C4 in purple. The orthosteric binding site is enlarged and further rotated by 90 °C in the right panels. Residues involved in nicotine binding are depicted in sticks. e Side view of the C4-Nic structure, represented in cartoon with α7 in pink and C4 in purple. The orthosteric binding site is enlarged and further rotated by 90 °C in the right panels. Residues involved in nicotine binding and nicotine itself are depicted in sticks.

Back to article page