Fig. 3: E3-α7 cryo-EM structures in the absence or presence of nicotine. | Nature Communications

Fig. 3: E3-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. 3: E3-α7 cryo-EM structures in the absence or presence of nicotine.The alternative text for this image may have been generated using AI.

a Unsharpened maps of the α7∆ICDcryo in complex with E3-Apo (left) and E3-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 E3-Apo structure, protein chains are depicted in white (α7 apo-) and green (E3). The orthosteric sites are shown in (c). c Neurotransmitter binding pocket of E3-Nic and E3-Apo. Electron densities are contoured at 7σ, and residues involved in neurotransmitter binding are shown in sticks. Nicotine was built in the extra density found in E3Nic, while the small and spherical density found in E3-Apo likely fits a cation or a water molecule. d Side view of the E3-Apo structure, represented in cartoon with α7 in white and E3 in green. 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 E3-Nic structure, represented in cartoon with α7 in pink and E3 in green. 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.

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