Structural features of serotonin 5-HT3 receptors in native and modified formsстатьяТезисы
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Аннотация:Popinako A., Antonov M., Shaitan K. Structural features of serotonin 5-HT3 receptors in native and modified forms. FEBS Journal 278 (Suppl. 1) 74–445 (2011), pp. 127.
ТЕЗИСЫ P03.117
http://onlinelibrary.wiley.com/store/10.1111/j.1742-4658.2011.08137.x/asset/j.1742-4658.2011.08137.x.pdf;jsessionid=43DCB8525D2BFF256F5836716A415508.f01t02?v=1&t=i8n7lh2p&s=4cd1a5523d5383dc93c3cd265a2a1adf159a424d
Serotonin 5-HT3 receptors are members of the Cys-loop superfamily of ligand-gated ion channels which exhibit important
physiological functions. 5-HT3 receptors structure investigation is necessary for better understanding of their role in different neurophysiological processes. The modifications of 5-HT3 receptors may lead to various pathologies (psychiatric disorders). Here we
present models of 5-HT3 receptors constructed from a homology structure of nACh, and discuss the amino acid sequence responsible
for their different activities. The molecular models of 5-HT3 receptors were created using MODELLER program. Some
amino acid residues responsible for the different activities were investigated by the method of molecular dynamics. We used
GROMACS software for characterization of amino acid substitutions occurring in 5-HT3 receptor molecule. Our models of 5-
HT3 receptors have demonstrated that extracellular domains are rich of negative charge that may be responsible for cation migration
into the cell. It was shown that the steric factor of THR289 hampers the cation transmission. The energy profile analysis has
demonstrated the energy minimum presence in the region that is 2 nm apart from the mouth of the channel. Apparently, it is the
region of negative-charged amino acids GLU272, ASP293 that takes part in the cation hydrate coat reorganization. We observed
that ligand binding for the native form of the 5-HT3 receptor is energetically more favorable than those for modified forms. Our
results reveal the relationship between the structure and the different activities of the serotonin 5-HT3 receptors and may be
useful in neurophysiological and pharmacological studies.