Abstract:
:Members of the transient receptor potential (TRP) ion channels conduct cations into cells. They mediate functions ranging from neuronally mediated hot and cold sensation to intracellular organellar and primary ciliary signaling. Here we report a cryo-electron microscopy (cryo-EM) structure of TRPC4 in its unliganded (apo) state to an overall resolution of 3.3 Å. The structure reveals a unique architecture with a long pore loop stabilized by a disulfide bond. Beyond the shared tetrameric six-transmembrane fold, the TRPC4 structure deviates from other TRP channels with a unique cytosolic domain. This unique cytosolic N-terminal domain forms extensive aromatic contacts with the TRP and the C-terminal domains. The comparison of our structure with other known TRP structures provides molecular insights into TRPC4 ion selectivity and extends our knowledge of the diversity and evolution of the TRP channels.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Duan J,Li J,Zeng B,Chen GL,Peng X,Zhang Y,Wang J,Clapham DE,Li Z,Zhang Jdoi
10.1038/s41467-018-05247-9subject
Has Abstractpub_date
2018-08-06 00:00:00pages
3102issue
1issn
2041-1723pii
10.1038/s41467-018-05247-9journal_volume
9pub_type
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