The existence of a second allosteric site on the M1 muscarinic acetylcholine receptor and its implications for drug design

L. Michel Espinoza-Fonseca, José G. Trujillo-Ferrara

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1217-1220
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume16
Issue number5
DOIs
StatePublished - Mar 1 2006

Bibliographical note

Funding Information:
The authors thank Edward C. Hulme for kindly providing the coordinates of the homology model of the M 1 muscarinic receptor and Asya Varbanova for her careful review of the manuscript. This work was supported by grants from CONACYT and CGPI-IPN to J.G.T.F and from the Department of Biochemistry, Structural Biology and Biophysics, University of Minnesota, and the Minnesota Supercomputing Institute to L.M.E.F.

Keywords

  • Alzheimer's disease
  • Blind docking
  • M muscarinic receptor
  • Molecular dynamics simulations
  • Multiple allosteric sites
  • Relax complex scheme
  • Staurosporine derivatives

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