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TitleStructural insight into the assembly of TRPV channels.
Journal, issue, pagesStructure, Vol. 22, Issue 2, Page 260-268, Year 2014
Publish dateFeb 4, 2014
AuthorsKevin W Huynh / Matthew R Cohen / Sudha Chakrapani / Heather A Holdaway / Phoebe L Stewart / Vera Y Moiseenkova-Bell /
PubMed AbstractTransient receptor potential (TRP) proteins are a large family of polymodal nonselective cation channels. The TRP vanilloid (TRPV) subfamily consists of six homologous members with diverse functions. ...Transient receptor potential (TRP) proteins are a large family of polymodal nonselective cation channels. The TRP vanilloid (TRPV) subfamily consists of six homologous members with diverse functions. TRPV1-TRPV4 are nonselective cation channels proposed to play a role in nociception, while TRPV5 and TRPV6 are involved in epithelial Ca²⁺ homeostasis. Here we present the cryo-electron microscopy (cryo-EM) structure of functional, full-length TRPV2 at 13.6 Å resolution. The map reveals that the TRPV2 cytoplasmic domain displays a 4-fold petal-like shape in which high-resolution N-terminal ankyrin repeat domain (ARD) structures can be unambiguously fitted. Fitting of the available ARD structures for other TRPV subfamily members into the TRPV2 EM map suggests that TRPV subfamily members have highly homologous structural topologies. These results allowed us to postulate a structural explanation for the functional diversity among TRPV channels and their differential regulation by proteins and ligands.
External linksStructure / PubMed:24373766 / PubMed Central
MethodsEM (single particle)
Resolution13.6 Å
Structure data

EMDB-5688:
Structural insight into the thermoTRPV channels assembly
Method: EM (single particle) / Resolution: 13.6 Å

Source
  • Rattus norvegicus (Norway rat)

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