Insights from modelling the 3D structure of the extracellular domain of alpha7 nicotinic acetylcholine receptor.
Based on the crystal structure of acetylcholine-binding protein, the three-dimensional structures of the extracellular domain, or the ligand-binding domains, of the monomer, homodimer, and homopentamer of the alpha7 nicotinic acetylcholine receptor were derived. The interface between two subunits, where the ligand-binding site is located, was investigated. Furthermore, an explicit definition of the ligand-binding pocket was illustrated that might provide useful clues for conducting various mutagenesis studies for finding drugs against schizophrenia and Alzheimer's disease.
Chou
Kuo-Chen
KC
Gordon Life Science Institute, San Diego, CA 92130, USA. lifescience@san.rr.com
D000595:Amino Acid Sequence; D019281:Dimerization; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011978:Receptors, Nicotinic / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D064569:alpha7 Nicotinic Acetylcholine Receptor
D011978:Receptors, Nicotinic; D064569:alpha7 Nicotinic Acetylcholine Receptor