The transient receptor potential classical or canonical (TRPC) 5 channel is a non-selective calcium-permeable cation channel that recently emerged as a promising target for the treatment of various diseases such as mental disorders and kidney diseases. Thus, detailed insight into the structural properties of TRPC5 channels is of utmost importance to further advance TRPC5 channels as drug targets. Recently, Song et al. (2021) have presented cryo-EM structures of the human TRPC5 channel alone or in complex with two different inhibitors thereby revealing two new distinct drug binding sites. Moreover, a binding site for the second messenger diacylglycerol (DAG) has been identified commensurate with a key role of DAG for TRPC5 channel activation.

瞬时受体潜在经典或规范（TRPC）5通道是一种非选择性的钙可渗透阳离子通道，最近已成为治疗各种疾病（如精神疾病和肾脏疾病）的有希望的靶标。因此，深入了解TRPC5通道的结构特性对于进一步推进TRPC5通道作为药物靶标至关重要。最近，Song等。（2021）已经提出了人的TRPC5通道的冷冻-EM结构单独或与两种不同的抑制剂复合，从而揭示了两个新的不同的药物结合位点。而且，已经鉴定出第二信使二酰基甘油（DAG）的结合位点与DAG对于TRPC5通道激活的关键作用相当。