Abstract
TRPV1 is a major nociceptor for plant toxins such as capsaicin and resiniferatoxin (RTX), protons and heat. Activation of TRPV1 is known to be allosteric. However, we found that RTX, a potent agonist binding to the same vanilloid binding pocket as capsaicin, opens TRPV1 to a much higher conductance state, as can be observed at both single-channel and macroscopic levels. Nonetheless, only one dominant conductance state can be observed in RTX-activated channels under physiological conditions. Unlike capsaicin, which rapidly and reversibly activates TRPV1, RTX induces slow and irreversible activation.
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