6cuc
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Solution structure of double knot toxin (DkTx)
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Structural highlights
FunctionDKTX_CYRSC Selectively activates the heat-activated TRPV1 channel. It binds to TRPV1 in an open state-dependent manner, trapping it there to produce irreversible currents (PubMed:20510930, PubMed:26880553, PubMed:27281200). It binds to the outer edge of the external pore of TRPV1 in a counterclockwise configuration, using a limited protein-protein interface and inserting hydrophobic residues into the bilayer (PubMed:26880553, PubMed:27281200). It also partitions naturally into membranes, with the two lobes exhibiting opposing energetics for membrane partitioning (K1) and channel activation (K2) (PubMed:26880553). In addition, the toxin disrupts a cluster of hydrophobic residues behind the selectivity filter that are critical for channel activation (PubMed:26880553).[1] [2] [3] References
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This page was last modified 10:40, 14 June 2023.