Evidence map›Paper›PMID 15454428›Full record

ArticleBiophysical journal2004

A model of voltage gating developed using the KvAP channel crystal structure.

Indira H Shrivastava, Stewart R Durell, H Robert Guy

Abstract readComparative StudyEvaluation StudyValidation Study
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Membrane mechanics as a probe of ion-channel gating mechanisms.Physical review. E, Statistical, nonlinear, and soft matter physics · 2008
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Voltage sensor conformations in the open and closed states in ROSETTA structural models of K(+) channels.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  16. Article
  17. Review
  18. S3b amino acid residues do not shuttle across the bilayer in voltage-dependent Shaker K+ channels.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  19. 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.

Indira H ShrivastavaLaboratory of Experimental and Computational Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-5567, USA.
Stewart R Durell
H Robert Guy

Funding

MEMBRANE PROTEIN MODELINGZ01BC008363 · BC · BASIC SCIENCES · PI GUY, HOMER ROBERT · 1996 to 2005
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6 · The paper itself

Abstract

Having inspected the crystal structure of the complete KvAP channel protein, we suspect that the voltage-sensing domain is too distorted to provide reliable information about its native tertiary structure or its interactions with the central pore-forming domain. On the other hand, a second crystal structure of the isolated voltage-sensing domain may well correspond to a native open conformation. We also observe that the paddle model of gating developed from these two structures is inconsistent with many experimental results, and suspect it to be energetically unrealistic. Here we show that the isolated voltage-sensing domain crystal structure can be docked onto the pore domain portion of the full-length KvAP crystal structure in an energetically favorable way to create a model of the open conformation. Using this as a starting point, we have developed rather conventional models of resting and transition conformations based on the helical screw mechanism for the transition from the open to the resting conformation. Our models are consistent with both theoretical considerations and experimental results.

Indexed as

Ion Channel GatingModels, ChemicalModels, MolecularAmino Acid SequenceCell MembraneComputer SimulationCrystallographyMolecular Sequence DataMotionPorosityPotassium ChannelsPotassium Channels, Voltage-GatedProtein ConformationProtein Structure, TertiaryShaker Superfamily of Potassium ChannelsStructure-Activity RelationshipPotassium ChannelsPotassium Channels, Voltage-GatedShaker Superfamily of Potassium Channels

Identifiers

PMID15454428
PMCPMC1304651

What OpenQuestion holds

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Read underepoch 390

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.