A.O. Kovalevsky Institute of Biology of the South Seas of the RAS
Sevastopol State University
Sevastopol, Sevastopol, Russian Federation
Sevastopol, Sevastopol, Russian Federation
Sevastopol, Sevastopol, Russian Federation
Sevastopol, Sevastopol, Russian Federation
Acid-sensitive ion channels (ASICs) represent a family of membrane three subunits' DEG/ENaC proteins that transport Na+ ions and are found in representatives of many taxonomic groups [1]. DEG/EnaC channels include such structural domains as the palm, β-ball, knuckle, finger, thumb and wrist [2]. They are involved in many physiological processes as proton-regulated channels, when the pH of the extracellular environment changes [3]. DEG/ENaC channels are associated with a wide range of cellular functions, such as pain sensation and epithelial Na+ transport [4]. These channels have different gating properties, from almost constant opening to rapid inactivation, so numerous pathologies are associated with damage to these channels [5]. Traditionally, the functions of these channels have been studied using toxins [6]. We found 9 acid-sensitive ion channel genes and 12 homologs with unknown function in the Trichoplax adhaerens genome, of which two amino acid sequences (QEP99390.1 and XP_002115321.1) were folded into 3D-models and used to dock amiloride, aspirin and salicylic acid. Salicylates have multiple binding sites on the acid-sensitive trichoplax receptors, including the acid pocket that is a proton sensor, which suggests their possible application in modulating the activity of the ASIC-channels of T. adhaerens.
Placozoa, genome, ASIC channels, homology, folding, docking
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