6ot5

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Structure of the TRPV3 K169A sensitized mutant in the presence of 2-APB at 3.6 A resolution

Structural highlights

6ot5 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.6Å
Experimental data:Check to display Experimental Data
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

TRPV3_HUMAN Mutilating palmoplantar keratoderma with periorificial keratotic plaques. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.

Function

TRPV3_HUMAN Putative receptor-activated non-selective calcium permeant cation channel. It is activated by innocuous (warm) temperatures and shows an increased response at noxious temperatures greater than 39 degrees Celsius. Activation exhibits an outward rectification. May associate with TRPV1 and may modulate its activity. Is a negative regulator of hair growth and cycling: TRPV3-coupled signaling suppresses keratinocyte proliferation in hair follicles and induces apoptosis and premature hair follicle regression (catagen).[1] [2] [3]

Publication Abstract from PubMed

Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are activated by ligands and heat, and are involved in various physiological processes. ThermoTRPV channels possess a large cytoplasmic ring consisting of N-terminal ankyrin repeat domains (ARD) and C-terminal domains (CTD). The cytoplasmic inter-protomer interface is unique and consists of a CTD coiled around a b-sheet which makes contacts with the neighboring ARD. Despite much existing evidence that the cytoplasmic ring is important for thermoTRPV function, the mechanism by which this unique structure is involved in thermoTRPV gating has not been clear. Here we present cryo-EM and electrophysiological studies which demonstrate that TRPV3 gating involves large rearrangements at the cytoplasmic inter-protomer interface and that this motion triggers coupling between cytoplasmic and transmembrane domains, priming the channel for opening. Furthermore, our studies unveil the role of this interface in the distinct biophysical and physiological properties of individual thermoTRPV subtypes.

Regulatory switch at the cytoplasmic interface controls TRPV channel gating.,Zubcevic L, Borschel WF, Hsu AL, Borgnia MJ, Lee SY Elife. 2019 May 9;8. pii: 47746. doi: 10.7554/eLife.47746. PMID:31070581[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. ↑ Xu H, Ramsey IS, Kotecha SA, Moran MM, Chong JA, Lawson D, Ge P, Lilly J, Silos-Santiago I, Xie Y, DiStefano PS, Curtis R, Clapham DE. TRPV3 is a calcium-permeable temperature-sensitive cation channel. Nature. 2002 Jul 11;418(6894):181-6. Epub 2002 Jun 23. PMID:12077604 doi:http://dx.doi.org/10.1038/nature00882
  2. ↑ Smith GD, Gunthorpe MJ, Kelsell RE, Hayes PD, Reilly P, Facer P, Wright JE, Jerman JC, Walhin JP, Ooi L, Egerton J, Charles KJ, Smart D, Randall AD, Anand P, Davis JB. TRPV3 is a temperature-sensitive vanilloid receptor-like protein. Nature. 2002 Jul 11;418(6894):186-90. doi: 10.1038/nature00894. Epub 2002 Jun 23. PMID:12077606 doi:http://dx.doi.org/10.1038/nature00894
  3. ↑ Borbiro I, Lisztes E, Toth BI, Czifra G, Olah A, Szollosi AG, Szentandrassy N, Nanasi PP, Peter Z, Paus R, Kovacs L, Biro T. Activation of transient receptor potential vanilloid-3 inhibits human hair growth. J Invest Dermatol. 2011 Aug;131(8):1605-14. doi: 10.1038/jid.2011.122. Epub 2011 , May 19. PMID:21593771 doi:http://dx.doi.org/10.1038/jid.2011.122
  4. ↑ Zubcevic L, Borschel WF, Hsu AL, Borgnia MJ, Lee SY. Regulatory switch at the cytoplasmic interface controls TRPV channel gating. Elife. 2019 May 9;8. pii: 47746. doi: 10.7554/eLife.47746. PMID:31070581 doi:http://dx.doi.org/10.7554/eLife.47746

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6ot5, resolution 3.60Å

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