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Cysteine modification reveals which subunits form the ligand binding site in human heteromeric 5‐HT 3 AB receptors
Author(s) -
Thompson A. J.,
Price K. L.,
Lummis S. C. R.
Publication year - 2011
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2011.208439
Subject(s) - cysteine , chemistry , receptor , binding site , biophysics , posttranslational modification , ligand (biochemistry) , biochemistry , stereochemistry , biology , enzyme
Non‐technical summary Nerve signals are transmitted across cell membranes by receptors that can consist of multiple different subunits. The 5‐HT 3 receptor is a pentamer which can function with A subunits alone, or with a mixture of A and B subunits. As 5‐HT activates the receptor by binding at the interface of adjacent subunits, it is important to know which subunits are adjacent. Here we show that in both A‐only and A+B receptors there is at least one A–A interface, without which the receptor cannot function. This knowledge is important for understanding the receptor mechanism, and also will allow the design of more specific drugs that act at the 5‐HT binding site.