The existence of a second allosteric site on the M1 muscarinic acetylcholine receptor and its implications for drug design.
Fully flexible docking of KT5720, an allosteric modulator of the muscarinic receptors, was performed on a dynamic model of the M(1) muscarinic acetylcholine receptor. The results confirmed the existence of a second allosteric site, located on the intracellular face of the receptor. These results would be beneficial for the design of modulators of this receptor to be used as an effective alternative against the Alzheimer's disease.
Espinoza-Fonseca
L Michel
LM
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA. mef@ddt.biochem.umn.edu
Trujillo-Ferrara
José G
JG
D000495:Allosteric Site; D002227:Carbazoles / Q000737:chemistry* / Q000378:metabolism*; D015195:Drug Design; D007211:Indoles / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D011758:Pyrroles / Q000737:chemistry* / Q000378:metabolism*; D043643:Receptor, Muscarinic M1 / Q000737:chemistry* / Q000378:metabolism*
D002227:Carbazoles; D007211:Indoles; D011758:Pyrroles; D043643:Receptor, Muscarinic M1; C057416:KT 5720