| Summary: | This dissertation concerns with characterization of binding sites for calcium binding protein S100A1 and phosphatidylinositol phosphates on intracellular regions of transient receptor potential channels (TRPs), particular from canonical (TRPC), vaniloid (TRPV) and melastatin (TRPM) families. TRPs represent superfamily of important mediators that play critical roles in sensory physiology: contributions to taste, olfaction, vision, hearing, touch and thermo- and osmo- sensation. They serve as non-selective and nociceptive membrane receptors responsible for the modulation of driving force for cations entry into the cell. TRPs are composed from six transmembrane domains and N- and C- termini intracellular regions. Overall four monomer units form a characteristic assembly of functional channel. It was demonstrated that most of this almost thirty-member family transporters are activated by a variety of different stimuli and function as signal integrators. The most examined intracellular TRPs modulators are cytosolic calcium binding proteins and membrane anchored phosphatidylinositol phosphates (PIPs). These signal integrators bind specific domains in intracellular termini of TRPs, thereby change their structure and activate or inhibit the transportation function of receptor. To identify a novel ligand...
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