Non-charged amino acids from three different domains contribute to link agonist binding to channel gating in α7 nicotinic acetylcholine receptors
Author:
Publisher
Wiley
Subject
Cellular and Molecular Neuroscience,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1471-4159.2007.04771.x/fullpdf
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4. Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors;Brejc;Nature,2001
5. A single residue in the M2-M3 loop is a major determinant of coupling between binding and gating in neuronal nicotinic receptors;Campos-Caro;Proc. Natl Acad. Sci. USA,1996
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2. Acetylcholine nicotinic receptor subtypes in chromaffin cells;Pflügers Archiv - European Journal of Physiology;2017-08-08
3. Mutants of β-strand β3 and the loop B in the interface between α7 subunits of a homomeric acetylcholine receptor show functional and pharmacological alterations;Journal of Neurochemistry;2011-08-08
4. Rapid desensitization of the rat α7 nAChR is facilitated by the presence of a proline residue in the outer β-sheet;The Journal of Physiology;2010-11-15
5. Role of the extracellular transmembrane domain interface in gating and pharmacology of a heteromeric neuronal nicotinic receptor;Journal of Neurochemistry;2010-05
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