Structural characterization of agonist and antagonist-bound acetylcholine-binding protein from Aplysia californica. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Molecular Neuroscience Année : 2006

Structural characterization of agonist and antagonist-bound acetylcholine-binding protein from Aplysia californica.

Scott B Hansen
  • Fonction : Auteur
Gerlind Sulzenbacher
Tom Huxford
  • Fonction : Auteur
Pascale Marchot
Yves Bourne
Palmer Taylor
  • Fonction : Auteur

Résumé

Nicotinic acetylcholine receptors (nAChRs) are well-characterized allosteric transmembrane proteins involved in the rapid gating of ions elicited by ACh. These receptors belong to the Cys-loop superfamily of ligand-gated ion channels, which also includes GABAA and GABAC, 5-HT3, and glycine receptors. The nAChRs are homo- or heteromeric pentamers of structurally related subunits that encompass an extracellular N-terminal ligand-binding domain, four transmembrane-spanning regions that form the ion channel, and an extended intracellular region between spans 3 and 4. Ligand binding triggers conformational changes that are transmitted to the transmembrane-spanning region, leading to gating and changes in membrane potential. The four transmembrane spans on each of the five subunits create a substantial region of hydrophobicity that precludes facile crystallization of this protein. However the freshwater snail, Lymnaea stagnalis, produces a soluble homopentameric protein, termed the ACh-binding protein (AChBP), which binds ACh (Smit et al., 2001). Its structure was determined recently (Brejc et al., 2001) at high resolution, revealing the structural scaffold for nAChR, and has become a functional and structural surrogate of the nAChR ligand-binding domain. We have characterized an AChBP from Aplysia californica and determined distinct ligand-binding properties when compared to those of L. stagnalis, including ligand specificity for the nAChR alpha7 subtype-specific alpha-conotoxin ImI (Hansen et al., 2004).
Fichier non déposé

Dates et versions

hal-00134314 , version 1 (01-03-2007)

Identifiants

  • HAL Id : hal-00134314 , version 1
  • PUBMED : 17192647

Citer

Scott B Hansen, Gerlind Sulzenbacher, Tom Huxford, Pascale Marchot, Yves Bourne, et al.. Structural characterization of agonist and antagonist-bound acetylcholine-binding protein from Aplysia californica.. Journal of Molecular Neuroscience, 2006, 30 (1-2), pp.101-2. ⟨hal-00134314⟩

Collections

CNRS UNIV-AMU
24 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More