Evidence map›Paper›PMID 28461506›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Molecular mechanism of multispecific recognition of Calmodulin through conformational changes.

Fei Liu, Xiakun Chu, H Peter Lu, Jin Wang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. 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
2.6field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
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  3. Review
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  6. Review
  7. Assessing the Role of Calmodulin's Linker Flexibility in Target Binding.International journal of molecular sciences · 2021
    Article
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  9. Article
  10. Article
  11. Article
  12. CaFrontiers in plant science · 2020
    Review
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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

4 authors at 4 institutions in 2 countries.

Fei LiuCollege of Physics, Jilin University, Changchun, Jilin, People's Republic of China 130012.
Xiakun ChuCollege of Physics, Jilin University, Changchun, Jilin, People's Republic of China 130012.
H Peter LuCenter for Photochemical Sciences, Department of Chemistry, Bowling Green State University, Bowling Green, OH 43403.
Jin WangCollege of Physics, Jilin University, Changchun, Jilin, People's Republic of China 130012; jin.wang.1@stonybrook.edu.
Bowling Green State University · USChangchun Institute of Applied Chemistry · CNJilin University · CNState University of New York · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calmodulin (CaM) is found to have the capability to bind multiple targets. Investigations on the association mechanism of CaM to its targets are crucial for understanding protein-protein binding and recognition. Here, we developed a structure-based model to explore the binding process between CaM and skMLCK binding peptide. We found the cooperation between nonnative electrostatic interaction and nonnative hydrophobic interaction plays an important role in nonspecific recognition between CaM and its target. We also found that the conserved hydrophobic anchors of skMLCK and binding patches of CaM are crucial for the transition from high affinity to high specificity. Furthermore, this association process involves simultaneously both local conformational change of CaM and global conformational changes of the skMLCK binding peptide. We found a landscape with a mixture of the atypical "induced fit," the atypical "conformational selection," and "simultaneously binding-folding," depending on the synchronization of folding and binding. Finally, we extend our discussions on multispecific binding between CaM and its targets. These association characteristics proposed for CaM and skMLCK can provide insights into multispecific binding of CaM.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCalciumCalmodulinComputer SimulationHumansHydrophobic and Hydrophilic InteractionsMyosin-Light-Chain KinaseProtein BindingProtein ConformationProtein FoldingProtein Interaction Domains and MotifsCalciumCalmodulinMyosin-Light-Chain KinaseCalmodulinmixture binding mechanismmultispecific recognitionstructure-based model

Identifiers

PMID28461506
PMCPMC5441799
OpenAlexW2610231528

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.