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Recent Structural and Mechanistic Insights into Endplate Acetylcholine Receptors
Author(s) -
Sine Steven M.,
Gao Fan,
Lee Won Yong,
Mukhtasimova Nuriya,
Wang HaiLong,
Engel Andrew G.
Publication year - 2008
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1405.041
Subject(s) - acetylcholine receptor , torpedo , gating , chemistry , acetylcholine , ion channel , biophysics , neuromuscular junction , receptor , neuroscience , biochemistry , biology , endocrinology
Voluntary movement mediated by skeletal muscle relies on endplate acetylcholine receptors (AChR) to detect nerve‐released ACh and depolarize the muscle fiber. Recent structural and mechanistic studies of the endplate AChR have catalyzed a leap in our understanding of the molecular steps in this chemical‐to‐electrical transduction process. Studies of acetylcholine binding protein (AChBP) give insight into ACh recognition, the first step in activation of the AChR. An atomic structural model of the Torpedo AChR at a resolution of 0.4 nm, together with single‐ion channel recording methods, allow tracing of the link between the agonist binding event and gating of the ion channel, as well as determination of how the channel moves when it opens to allow flow of cations. Structural models of the human AChR enable precise mapping of disease‐causing mutations, while studies of the speed with which single AChR channels open and close cast light on pathogenic mechanisms.