Evidence map›Paper›PMID 20923659›Full record

ArticleBiophysical journal2010

Allosteric response is both conserved and variable across three CheY orthologs.

James M Mottonen, Donald J Jacobs, Dennis R Livesay

Abstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

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  15. Ensemble properties of network rigidity reveal allosteric mechanisms.Methods in molecular biology (Clifton, N.J.) · 2012
    Article
  16. Article
  17. Ensemble-based methods for describing protein dynamics.Current opinion in pharmacology · 2010
    Review
  18. 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

3 authors.

James M MottonenDepartment of Physics and Optical Science, University of North Carolina, Charlotte, NC, USA.
Donald J Jacobs
Dennis R Livesay

Funding

NIGMS NIH HHS R01 GM070382
6 · The paper itself

Abstract

A computational method to identify residues likely to initiate allosteric signals has been developed. The method is based on differences within stability and flexibility profiles between wild-type and perturbed structures as computed by a distance constraint model. Application of the approach to three bacterial chemotaxis protein Y (CheY) orthologs provides a comparison of allosteric response across protein family divergence. Interestingly, we observe a rich mixture of both conservation and variability within the identified allosteric sites. While similarity within the overall response parallels the evolutionary relationships, >50% of the best scoring putative sites are only identified in a single ortholog. These results suggest that detailed descriptions of intraprotein communication are substantially more variable than structure and function, yet do maintain some evolutionary relationships. Finally, structural clusters of large response identify four allosteric hotspots, including the β4/α4 loop known to be critical to relaying the CheY phosphorylation signal.

Indexed as

Allosteric SiteConserved SequenceSequence Homology, Amino AcidAllosteric RegulationAmino Acid SequenceBacteriaBacterial ProteinsCatalytic DomainEscherichia coliEscherichia coli ProteinsEvolution, MolecularMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsModels, MolecularMolecular Sequence DataSalmonella typhimuriumBacterial ProteinscheY protein, E coliEscherichia coli ProteinsMembrane ProteinsMethyl-Accepting Chemotaxis Proteins

Identifiers

PMID20923659
PMCPMC3042579

What OpenQuestion holds

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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.