Abstract
A homology model of the human α7 nicotinic receptor was constructed based on the acetylcholine-binding protein crystal structure. Subsequently, the three-dimensional structure of the complex between the α7 nicotinic receptor and the 42-amino acid β-amyloid peptide was obtained for the first time with the aid of the ESCHER program, a well-known method for protein–protein docking. The final complex showed that the most important interactions occur between the residues V12–K28 from the peptide and the loop C of the receptor. The model agrees with many experimental data, and may be used as a base model for further detailed studies in order to gain insight into the binding and dynamics of the complex at molecular level and their correlation with the memory impairments characteristic of the Alzheimer’s disease.
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