Evidence map›Paper›PMID 15879477›Full record

ArticleBiophysical journal2005

Probing the local dynamics of nucleotide-binding pocket coupled to the global dynamics: myosin versus kinesin.

Wenjun Zheng, Bernard R Brooks

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.0field-weighted citation impact, top 6% of its field
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

41 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Protein dynamics developments for the large scale and cryoEM: case study of ProDy 2.0.Acta crystallographica. Section D, Structural biology · 2022
    Review
  6. Article
  7. Article
  8. Structural Communication between theInternational journal of molecular sciences · 2021
    Article
  9. Article
  10. Review
  11. Structural basis for power stroke vs. Brownian ratchet mechanisms of motor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Review
  13. Simple mechanics of protein machines.Journal of the Royal Society, Interface · 2019
    Article
  14. Article
  15. Article
  16. Protein dynamics and the all-ferrous [Fe4 S4 ] cluster in the nitrogenase iron protein.Protein science : a publication of the Protein Society · 2016
    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

2 authors at 1 institution in 1 country.

Wenjun ZhengLaboratory of Computational Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, USA. zhengwj@helix.nih.gov
Bernard R Brooks
National Institutes of Health · US

Funding

Development Of Theoretical Methods For Studying Biological MacromoleculesZIAHL001051 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI BROOKS, BERNARD R · 2009 to 2025
$16.2M
Molecular Dynamics Simulations Of Biological MacromoleculesZIAHL001050 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI BROOKS, BERNARD R · 2009 to 2025
$12.9M
Molecular Dynamics Simulations of MacromoleculesZ01HL001050 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI BROOKS, BERNARD R · 1998 to 2008
$1.4M
Theoretical Methods to Study Biological MacromoleculesZ01HL001051 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI BROOKS, BERNARD R · 1998 to 2008
$1.4M
6 · The paper itself

Abstract

Based on the elastic network model, we develop a new analysis for protein complexes, which probes the local dynamics of a subsystem that is elastically coupled to a fluctuating environment. This method is applied to a comparative dynamical analysis of the nucleotide-binding pocket of two motor proteins-myosins and kinesins. In myosins, the observed structural changes in the nucleotide-pocket from the transition state to the rigorlike state are dominated by the lowest normal mode that involves significant movements in both switch I and switch II; in kinesins, the measured conformational changes in the nucleotide-pocket are also dominated by the lowest mode, which, however, only involves large movement in switch I. We then compute the global structural changes induced by the nucleotide-pocket deformations as described by the dominant pocket-mode, which yield encouraging results: in myosins, multiple hinge motions involving the opening/closing of the cleft between the upper and lower 50 -kDa subdomains and the swinging movement of the converter are induced, which are dominated by precisely the same global mode that has been recently identified by us as important to the dynamical correlations among the nucleotide-pocket, the actin-binding site, and the converter; in kinesins, the induced global conformational changes are well described by a highly collective global mode which hints for a dynamical pathway spanning from the nucleotide-pocket to the neck-linker via the H6 helix.

Indexed as

ActinsAnimalsBinding SitesCrystallography, X-RayHumansKinesinsLigandsModels, MolecularModels, StatisticalMolecular ConformationMyosinsNucleotidesPrincipal Component AnalysisProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryActinsKinesinsLigandsMyosinsNucleotides

Identifiers

PMID15879477
PMCPMC1366515
OpenAlexW2052612332

What OpenQuestion holds

Textmetadata
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.