Evidence map›Paper›PMID 16326912›Full record

ArticleBiophysical journal2006

The intrinsic flexibility of the Kv voltage sensor and its implications for channel gating.

Zara A Sands, Alessandro Grottesi, Mark S P Sansom

Abstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

21 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Detergent-mediated protein aggregation.Chemistry and physics of lipids · 2013
    Review
  8. Review
  9. Article
  10. Potassium channel opening: a subtle two-step.The Journal of physiology · 2009
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Bilayer deformation by the Kv channel voltage sensor domain revealed by self-assembly simulations.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  17. Article
  18. Article
  19. A voltage-sensor water pore.Biophysical journal · 2006
    Article
  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

3 authors.

Zara A SandsDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
Alessandro Grottesi
Mark S P Sansom

Funding

Biotechnology and Biological Sciences Research Council B19456Biotechnology and Biological Sciences Research Council BBS/B/16011Biotechnology and Biological Sciences Research Council BEP17032Wellcome Trust
6 · The paper itself

Abstract

Analysis of the crystal structures of the intact voltage-sensitive potassium channel KvAP (from Aeropyrum pernix) and Kv1.2 (from rat brain), along with the isolated voltage sensor (VS) domain from KvAP, raises the question of the exact nature of the voltage-sensing conformational change that triggers activation of Kv and related voltage-gated channels. Molecular dynamics simulations of the isolated VS of KvAP in a detergent micelle environment at two different temperatures (300 K and 368 K) have been used to probe the intrinsic flexibility of this domain on a tens-of-nanoseconds timescale. The VS contains a positively charged (S4) helix which is packed against a more hydrophobic S3 helix. The simulations at elevated temperature reveal an intrinsic flexibility/conformational instability of the S3a region (i.e., the C-terminus of the S3 helix). It is also evident that the S4 helix undergoes hinge bending and swiveling about its central I130 residue. The conformational instability of the S3a region facilitates the motion of the N-terminal segment of S4 (i.e., S4a). These simulations thus support a gating model in which, in response to depolarization, an S3b-S4a "paddle" may move relative to the rest of the VS domain. The flexible S3a region may in turn act to help restore the paddle to its initial conformation upon repolarization.

Indexed as

Ion Channel GatingModels, ChemicalModels, MolecularComputer SimulationDetergentsElasticityPorosityPotassium Channels, Voltage-GatedProtein ConformationProtein Structure, TertiaryTemperatureWaterDetergentsPotassium Channels, Voltage-GatedWater

Identifiers

PMID16326912
PMCPMC1367311

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

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.