Transient receptor potential (TRP) channels are a wide family of non-selective ion channels responsible for monovalent and divalent cation influx into the cells. Members of this family are involved in many sensory processes such as invertebrate vision and hearing, mammalian temperature-, mechano- and chemo-sensation. The TRP channels discovered so far can be divided into seven subfamilies according to their primary structure: TRPV, TRPC, TRPA, TRPM, TRPP, TRPML and TRPN. All are predicted to have six transmembrane helices (S1–S6) and a pore-forming loop between S5 and S6, with varying sizes of intracellular amino and carboxy termini, and are thought to form tetrameric assemblies. Both the N- and C-terminal intracellular domains are comprised of many different domains that are responsible for binding different compounds that can regulate the channels. Our goal is to provide the structural insight into the interactions of TRP channels with ATP, calmodulin and PIP.

Results

We identified two basic amino acids R755 and R767 on the N-terminus of TRPM4 channel that interact with the PIP2/PIP3 molecules directly. 

Schematic view and the solvent accessible surface representation of the interactions of TRPM4 733-772/PIP2. (Boušová et al. 2015).