Title of article :
The existence of a second allosteric site on the M1 muscarinic acetylcholine receptor and its implications for drug design
Author/Authors :
L. Michel Espinoza-Fonseca، نويسنده , , José G. Trujillo-Ferrara، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2006
Abstract :
Fully flexible docking of KT5720, an allosteric modulator of the muscarinic receptors, was performed on a dynamic model of the M1 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.
Keywords :
Alzheimer’s disease , Staurosporine derivatives , Multiple allosteric sites , Relax complex scheme , Molecular dynamics simulations , M1 muscarinic receptor , Blind docking
Journal title :
Bioorganic & Medicinal Chemistry Letters
Journal title :
Bioorganic & Medicinal Chemistry Letters