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Contemporary paradigms for cholinergic ligand design guided by biological structure

Academic Article
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Overview

authors

  • Taylor, P.
  • Hansen, Scott
  • Talley, T. T.
  • Hibbs, R. E.
  • Radic, Z.

publication date

  • April 2004

journal

  • Bioorganic & Medicinal Chemistry Letters  Journal

abstract

  • The identification of the various nicotinic receptor subtypes, when coupled with the recent development of three-dimensional structures of surrogate extracellular receptor domains, offers new opportunities to design nicotinic ligands. Conformation and fluctuations in receptor structure are critical to ligand selectivity, and we present here how a flexible receptor template can be used in the development of selective ligands affecting cholinergic neurotransmission.

subject areas

  • Binding Sites
  • Drug Design
  • Ligands
  • Nicotinic Agonists
  • Protein Conformation
  • Receptors, Nicotinic
  • Structure-Activity Relationship
  • Time Factors
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Identity

PubMed Central ID

  • PMC3191913

International Standard Serial Number (ISSN)

  • 0960-894X

Digital Object Identifier (DOI)

  • 10.1016/j.bmcl.2003.10.072

PubMed ID

  • 15050619
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Additional Document Info

start page

  • 1875

end page

  • 1877

volume

  • 14

issue

  • 8

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