The transient receptor potential vanilloid receptor-1 (TRPV1) is a sensory neuron-specific nonselective cation channel that is gated in response to various noxious stimuli: pungent vanilloids, low pH, noxious heat, and depolarizing voltages. By its analogy to K+ channels, the S6 inner helix domain of TRPV1 (Y666-G683) is a prime candidate to form the most constricted region of the permeation pathway and might therefore encompass an as-yet-unmapped gate of the channel. Using alanine-scanning mutagenesis, we identified 16 of 17 residues, that when mutated affected the functionality of the TRPV1 channel with respect to at least one stimulus modality. T670A was the only substitution producing the wild-type channel phenotype, whereas Y666A and N676A were nonfunctional but present at the plasma membrane. The periodicity of the functional effects of mutations within the TRPV1 inner pore region is consistent with an alpha-helical structure in which T670 and A680 might play the roles of two bending "hinges."

• MeSH
• alanin MeSH
• buněčné linie MeSH
• elektrofyziologie MeSH
• gating iontového kanálu fyziologie   MeSH
• kapsaicin farmakologie   MeSH
• kationtové kanály TRPV chemie   účinky léků   genetika   fyziologie   MeSH
• krysa rodu Rattus MeSH
• lidé MeSH
• membránové potenciály MeSH
• mutace MeSH
• mutageneze cílená MeSH
• vysoká teplota MeSH
• zvířata MeSH
• Check Tag
• krysa rodu Rattus MeSH
• lidé MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• alanin MeSH
• kapsaicin MeSH
• kationtové kanály TRPV MeSH
• Trpv1 protein, rat MeSH Prohlížeč