Evidence map›Paper›PMID 24248473›Full record

ArticleProtein & cell2013

Crystal structure of the N-terminal ankyrin repeat domain of TRPV3 reveals unique conformation of finger 3 loop critical for channel function.

Di-Jing Shi, Sheng Ye, Xu Cao, Rongguang Zhang, KeWei Wang

Abstract read
In one paragraph

Article in Protein & cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. TRPV3 Ion Channel: From Gene to Pharmacology.International journal of molecular sciences · 2023
    Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Structural basis of temperature sensation by the TRP channel TRPV3.Nature structural & molecular biology · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Di-Jing ShiDepartment of Neurobiology, Neuroscience Research Institute, Peking University Health Science Center, Beijing, 100191, China.
Sheng Ye
Xu Cao
Rongguang Zhang
KeWei Wang

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In all six members of TRPV channel subfamily, there is an ankyrin repeat domain (ARD) in their intracellular N-termini. Ankyrin (ANK) repeat, a common motif with typically 33 residues in each repeat, is primarily involved in protein-protein interactions. Despite the sequence similarity among the ARDs of TRPV channels, the structure of TRPV3-ARD, however, remains unknown. Here, we report the crystal structure of TRPV3-ARD solved at 1.95 Å resolution, which reveals six-ankyrin repeats. While overall structure of TRPV3-ARD is similar to ARDs from other members of TRPV subfamily; it, however, features a noticeable finger 3 loop that bends over and is stabilized by a network of hydrogen bonds and hydrophobic packing, instead of being flexible as seen in known TRPV-ARD structures. Electrophysiological recordings demonstrated that mutating key residues R225, R226, Q255, and F249 of finger 3 loop altered the channel activities and pharmacology. Taken all together, our findings show that TRPV3-ARD with characteristic finger 3 loop likely plays an important role in channel function and pharmacology.

Indexed as

Amino Acid SequenceAnkyrin RepeatCrystallography, X-RayHEK293 CellsHumansModels, MolecularMolecular Sequence DataPatch-Clamp TechniquesProtein BindingProtein ConformationProtein Structure, TertiarySequence Homology, Amino AcidTRPV Cation ChannelsTRPV3 protein, humanTRPV Cation Channels

Identifiers

PMID24248473
PMCPMC4875401

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.