Abstract
The three-dimensional structure of the 5-HT3 receptor is currently unknown. An available structure of the nicotinic acetylcholine receptor closely related by homology to the 5-HT3 receptor was used as a template for the computer-based homology modeling of the 5-HT3 receptor. The study of the ion migration through the channel by the steered molecular dynamics method has shown that the steric factor in the region of residue Thr279 and the region of Glu272, Asp293 influences the ion transmission. The characteristic of the close interaction between the ion and the amino acid substitutions of the 5-HT3 channel was studied by computing the energy profile using constraint force molecular dynamic simulations. The amino acid sequence responsible for selective ion transmission has been investigated. The structure of the channel domain of the serotonin 5-HT3 receptor as a universal functional unit of the ligand-gated ion channels was discussed.
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Original Russian Text © A.V. Popinako, O.V. Levtsova, M.Yu. Antonov, I.N. Nikolaev, K.V. Shaitan, 2011, published in Biofizika, 2011, Vol. 56, No. 6, pp. 1111–1116.
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Popinako, A.V., Levtsova, O.V., Antonov, M.Y. et al. The structural and dynamic model of the serotonin 5-HT3 receptor. Comparative analysis of the structure of the channel domain of pentameric ligand-gated ion channels. BIOPHYSICS 56, 1078–1082 (2011). https://doi.org/10.1134/S0006350911060157
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DOI: https://doi.org/10.1134/S0006350911060157