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Research ArticleArticle

A Cation-π Interaction at a Phenylalanine Residue in the Glycine Receptor Binding Site Is Conserved for Different Agonists

Stephan A. Pless, Ariele P. Hanek, Kerry L. Price, Joseph W. Lynch, Henry A. Lester, Dennis A. Dougherty and Sarah C. R. Lummis
Molecular Pharmacology April 2011, 79 (4) 742-748; DOI: https://doi.org/10.1124/mol.110.069583

Article Information

vol. 79 no. 4 742-748
DOI 
https://doi.org/10.1124/mol.110.069583
PubMed 
21266487
Published By 
American Society for Pharmacology and Experimental Therapeutics
Print ISSN 
0026-895X
Online ISSN 
1521-0111
History 
  • Received October 22, 2010
  • Accepted January 4, 2011
  • Published online March 18, 2011.

Article Versions

Copyright & Usage 
Copyright © 2011 The American Society for Pharmacology and Experimental Therapeutics

Author Information

  1. Stephan A. Pless1,
  2. Ariele P. Hanek,
  3. Kerry L. Price,
  4. Joseph W. Lynch,
  5. Henry A. Lester,
  6. Dennis A. Dougherty and
  7. Sarah C. R. Lummis
  1. School of Biomedical Sciences and Queensland Brain Institute, University of Queensland, Brisbane, Queensland, Australia (S.A.P., J.W.L.); Division of Chemistry and Chemical Engineering (A.P.L., D.A.D.) and Biology (H.A.L.), California Institute of Technology, Pasadena, California; and Department of Biochemistry, University of Cambridge, Cambridge UK (K.L.P., S.C.R.L.)
  1. Address correspondence to:
    Sarah C. R. Lummis, Department of Biochemistry, Tennis Court Road, Cambridge CB2 1QW. E-mail: sl120{at}cam.ac.uk

  • ↵1 Current affiliation: Department of Anaesthesiology, Pharmacology and Therapeutics, University of British Columbia, Vancouver, BC, Canada.

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Research ArticleArticle

A Cation-π Interaction at a Phenylalanine Residue in the Glycine Receptor Binding Site Is Conserved for Different Agonists

Stephan A. Pless, Ariele P. Hanek, Kerry L. Price, Joseph W. Lynch, Henry A. Lester, Dennis A. Dougherty and Sarah C. R. Lummis
Molecular Pharmacology April 1, 2011, 79 (4) 742-748; DOI: https://doi.org/10.1124/mol.110.069583
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