TRPV1, a member of the transient receptor potential (TRP) channels family, has been found to be involved in redox sensing. The crystal structure of the human TRPV1 ankyrin‐repeat domain (TRPV1‐ARD) was determined at 4.5 Å resolution under nonreducing conditions. This is the first report of the crystal structure of a ligand‐free form of TRPV1‐ARD and in particular of the human homologue. The structure showed a unique conformation in finger loop 3 near Cys258, which is most likely to be involved in inter‐subunit disulfide‐bond formation. Also, in human TRPV1‐ARD it was possible for solvent to access Cys258. This structural feature might be related to the high sensitivity of human TRPV1 to oxidants. ESI‐MS revealed that Cys258 did not form an S–OH functionality even under nonreducing conditions.

中文翻译：

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在非还原条件下人TRPV1锚蛋白重复结构域的结构测定。

TRPV1是瞬时受体电位（TRP）通道家族的成员，已发现它参与氧化还原感测。在非还原条件下以4.5Å的分辨率确定了人类TRPV1锚蛋白重复结构域（TRPV1-ARD）的晶体结构。这是首次报告无配体形式的TRPV1-ARD，尤其是人类同源物的晶体结构。该结构在Cys258附近的指环3中显示出独特的构象，最有可能参与亚基间二硫键的形成。同样，在人类TRPV1-ARD中，溶剂可能会进入Cys258。这种结构特征可能与人类TRPV1对氧化剂的高敏感性有关。ESI-MS显示，即使在非还原条件下，Cys258也不形成S-OH功能。