Evidence map›Paper›PMID 15339800›Full record

ArticleBiophysical journal2004

Long-residency hydration, cation binding, and dynamics of loop E/helix IV rRNA-L25 protein complex.

Kamila Réblová, Nad'a Spacková, Jaroslav Koca, Neocles B Leontis, Jirí Sponer

Abstract readComparative StudyEvaluation 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 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. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Molecular dynamics simulations of nucleic acid-protein complexes.Current opinion in structural biology · 2008
    Review
  12. Article
  13. Review
  14. Article
  15. Trapped water molecules are essential to structural dynamics and function of a ribozyme.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  16. Article
  17. Article
  18. 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

5 authors.

Kamila RéblováNational Centre for Biomolecular Research, Faculty of Sciences, Masaryk University, Kotlárská 2, 61137 Brno, Czech Republic.
Nad'a Spacková
Jaroslav Koca
Neocles B Leontis
Jirí Sponer

Funding

SELECTION AND ANALYSIS OF STABLE RNA 3 WAY JUNCTIONSR15GM055898 · NIGMS · BOWLING GREEN STATE UNIVERSITY · PI LEONTIS, NEOCLES B · 1997 to 2010
$680k
NIGMS NIH HHS 2R15 GM55898NIGMS NIH HHS 3R15 GM55898NIGMS NIH HHS R15 GM055898
6 · The paper itself

Abstract

Molecular dynamics simulations of RNA-protein complex between Escherichia coli loop E/helix IV (LE/HeIV) rRNA and L25 protein reveal a qualitative agreement between the experimental and simulated structures. The major groove of LE is a prominent rRNA cation-binding site. Divalent cations rigidify the LE major groove geometry whereas in the absence of divalent cations LE extensively interacts with monovalent cations via inner-shell binding. The HeIV region shows bistability of its major groove explaining the observed differences between x-ray and NMR structures. In agreement with the experiments, the simulations suggest that helix-alpha1 of L25 is the least stable part of the protein. Inclusion of Mg2+ cations into the simulations causes perturbation of basepairing at the LE/HeIV junction, which does not, however, affect the protein binding. The rRNA-protein complex is mediated by a number of highly specific hydration sites with long-residing water molecules and two of them are bound throughout the entire 24-ns simulation. Long-residing water molecules are seen also outside the RNA-protein contact areas with water-binding times substantially enhanced compared to simulations of free RNA. Long-residency hydration sites thus represent important elements of the three-dimensional structure of rRNA.

Indexed as

Models, ChemicalModels, MolecularBinding SitesCationsComputer SimulationEscherichia coliMotionMultiprotein ComplexesNucleic Acid ConformationProtein BindingProtein ConformationRibosomal ProteinsRNA, BacterialRNA, RibosomalWaterCationsMultiprotein Complexesribosomal protein L25Ribosomal ProteinsRNA, BacterialRNA, RibosomalWater

Identifiers

PMID15339800
PMCPMC1304806

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.