西亚试剂：TRPV1 structures in distinct conformations reveal activatio

TRPV1 structures in distinct conformations reveal activation mechanisms

Erhu Cao，Maofu Liao，Yifan Cheng& David Julius

Transient receptor potential (TRP) channels are polymodal signal detectors that respond to a wide range of physical and chemical stimuli. Elucidating how these channels integrate and convert physiological signals into channel opening is essential to understanding how they regulate cell excitability under normal and pathophysiological conditions. Here we exploit pharmacological probes (a peptide toxin and small vanilloid agonists) to determine structures of two activated states of the capsaicin receptor， TRPV1. A domain (consisting of transmembrane segments 1–4) that moves during activation of voltage-gated channels remains stationary in TRPV1， highlighting differences in gating mechanisms for these structurally related channel superfamilies. TRPV1 opening is associated with major structural rearrangements in the outer pore， including the pore helix and selectivity filter， as well as pronounced dilation of a hydrophobic constriction at the lower gate， suggesting a dual gating mechanism. Allosteric coupling between upper and lower gates may account for rich physiological modulation exhibited by TRPV1 and other TRP channels.

• 以上资料由西亚试剂：http://www.xiyashiji.com/ 提供此产品的详细信息如密度,含量,分子式,分子量等均可在西亚官网查询   
• 相关产品如溴化汞硝酸亚汞氯化亚汞乙酸苯汞氯化钾汞 碘化汞钾硫氰酸汞硫酸亚汞氧化汞氯化汞碘化汞硝酸汞三氯氧磷三氯化磷碘甲烷二碘甲烷三碘甲烷三氟碘甲烷氘代碘甲烷碘乙烷1,2-二碘乙烷甲酸铷碘化铷溴化铷铬酸铷硫酸铷氟化铷硝酸铷氯化铷碳酸铷硫酸镱 碳酸镱氯化镱硝酸镱氧化镱等均有销售.欢迎订购