Evidence map›Paper›PMID 25416786›Full record

ArticleThe Journal of biological chemistry2015

Structural model of weak binding actomyosin in the prepowerstroke state.

Boglárka H Várkuti, Zhenhui Yang, Andras Malnasi-Csizmadia

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

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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.

Boglárka H VárkutiFrom the Department of Biochemistry, Institute of Biology and.
Zhenhui YangFrom the Department of Biochemistry, Institute of Biology and.
Andras Malnasi-CsizmadiaFrom the Department of Biochemistry, Institute of Biology and the ELTE-HAS Molecular Biophysics Research Group, Eötvös Loránd University, H-1117 Budapest and Optopharma Ltd., H-1015 Budapest, Hungary malnalab@yahoo.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present the first in silico model of the weak binding actomyosin in the initial powerstroke state, representing the actin binding-induced major structural changes in myosin. First, we docked an actin trimer to prepowerstroke myosin then relaxed the complex by a 100-ns long unrestrained molecular dynamics. In the first few nanoseconds, actin binding induced an extra primed myosin state, i.e. the further priming of the myosin lever by 18° coupled to a further closure of switch 2 loop. We demonstrated that actin induces the extra primed state of myosin specifically through the actin N terminus-activation loop interaction. The applied in silico methodology was validated by forming rigor structures that perfectly fitted into an experimentally determined EM map of the rigor actomyosin. Our results unveiled the role of actin in the powerstroke by presenting that actin moves the myosin lever to the extra primed state that leads to the effective lever swing.

Indexed as

Actin CytoskeletonActinsActomyosinBinding SitesDictyosteliumMolecular Dynamics SimulationMusclesMyosinsProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryThermodynamicsActinsActomyosinMyosinsActinEnzyme CycleEnzyme KineticsEnzyme MechanismMolecular DynamicsMyosinPowerstrokeProtein StructureStructural Model

Identifiers

PMID25416786
PMCPMC4340411

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.