Evidence map›Paper›PMID 20399184›Full record

ArticleStructure (London, England : 1993)2010

Rigor to post-rigor transition in myosin V: link between the dynamics and the supporting architecture.

Riina Tehver, D Thirumalai

Abstract read
PubMed Publisher
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024
    Article
  2. Article
  3. Article
  4. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  5. Structural Communication between theInternational journal of molecular sciences · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Kinematics of the lever arm swing in myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Simulating the dynamics of the mechanochemical cycle of myosin-V.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Article
  14. Conformational selection in protein binding and function.Protein science : a publication of the Protein Society · 2014
    Review
  15. Plasticity of hydrogen bond networks regulates mechanochemistry of cell adhesion complexes.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  16. Article
  17. Electrostatic origin of the unidirectionality of walking myosin V motors.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  18. Article
  19. Single-molecule nanometry for biological physics.Reports on progress in physics. Physical Society (Great Britain) · 2013
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Riina TehverBiophysics Program, Institute for Physical Science and Technology, University of Maryland, College Park, MD 20742, USA.
D Thirumalai

Funding

Molecular Basis for Protein Interactions with a Biological NanomachineF32GM082009 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI TEHVER, RIINA · 2007 to 2009
$147k
NIGMS NIH HHS 1 F32GM082009
6 · The paper itself

Abstract

The detachment kinetics from actin upon ATP binding is a key step in the reaction cycle of myosin V. We show that a network of residues, constituting the allostery wiring diagram (AWD), that trigger the rigor (R) to post-rigor (PR) transition, span key structural elements from the ATP and actin-binding regions. Several of the residues are in the 33 residue helix (H18), P loop, and switch I. Brownian dynamics simulations show that a hierarchy of kinetically controlled local structural changes leads to the opening of the "cleft" region, resulting in the detachment of the motor domain from actin. Movements in switch I and P loop facilitate changes in the rest of the motor domain, in particular the rotation of H18, whose stiffness within the motor domain is crucial in the R --> PR transition. The finding that residues in the AWD also drive the kinetics of the R --> PR transition shows how the myosin architecture regulates the allosteric movements during the reaction cycle.

Indexed as

ActinsAdenosine TriphosphateAllosteric SiteAmino Acid SequenceAnimalsComputer SimulationDictyosteliumKineticsModels, MolecularMolecular ConformationMolecular Sequence DataMyosinsMyosin Type VProtein BindingSequence Homology, Amino AcidSignal TransductionActinsAdenosine TriphosphateMyosinsMyosin Type V

Identifiers

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.