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Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence

Academic Article
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Overview

authors

  • Gao, F.
  • Bren, N.
  • Burghardt, T. P.
  • Hansen, Scott
  • Henchman, R. H.
  • Taylor, P.
  • McCammon, J. A.
  • Sine, S. M.

publication date

  • March 2005

journal

  • Journal of Biological Chemistry  Journal

abstract

  • We delineated acetylcholine (ACh)-dependent conformational changes in a prototype of the nicotinic receptor ligand binding domain by molecular dynamics simulation and changes in intrinsic tryptophan (Trp) fluorescence. Prolonged molecular dynamics simulation of ACh-binding protein showed that binding of ACh establishes close register of Trps from adjacent subunits, Trp(143) and Trp(53), and draws the peripheral C-loop inward to occlude the entrance to the binding cavity. Close register of Trp(143) and Trp(53) was demonstrated by ACh-mediated quenching of intrinsic Trp fluorescence, elimination of quenching by mutation of one or both Trps to Phe, and decreased lifetime of Trp fluorescence by bound ACh. Occlusion of the binding cavity by the C-loop was demonstrated by restricted access of an extrinsic quencher of binding site Trp fluorescence by ACh. The collective findings showed that ACh initially establishes close register of conserved Trps from adjacent subunits and then draws the C-loop inward to occlude the entrance to the binding cavity.

subject areas

  • Acetylcholine
  • Acrylamide
  • Animals
  • Binding Sites
  • Carrier Proteins
  • Crystallography, X-Ray
  • Humans
  • Ligands
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Snails
  • Spectrometry, Fluorescence
  • Time Factors
  • Tryptophan
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M412389200

PubMed ID

  • 15591050
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Additional Document Info

start page

  • 8443

end page

  • 8451

volume

  • 280

issue

  • 9

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