Evidence map›Paper›PMID 28282132›Full record

ArticleJournal of chemical theory and computation2017

Quantifying Allosteric Communication via Both Concerted Structural Changes and Conformational Disorder with CARDS.

Sukrit Singh, Gregory R Bowman

Open access · greenAbstract read
In one paragraph

Article in Journal of chemical theory and computation, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

50 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Mapping Allosteric Communication in the Nucleosome with Conditional Activity.Journal of chemical information and modeling · 2026
    Article
  3. Review
  4. Article
  5. Article
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  7. Article
  8. Review
  9. Discrete protein dynamics enable long-range communication.bioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. Article
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  13. PathogenicThe journal of physical chemistry. B · 2025
    Article
  14. Regulation of the ordinal DNA translocation cycle in bacteriophage Φ29 through trans-subunit interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
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  18. Article
  19. The G protein inhibitor YM-254890 is an allosteric glue.bioRxiv : the preprint server for biology · 2024
    Article
  20. SARS-CoV-2 3CLPro Dihedral Angles Reveal Allosteric Signaling.bioRxiv : the preprint server for biology · 2024
    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.

Sukrit SinghDepartment of Biochemistry and Molecular Biophysics, and ‡Center for Biological Systems Engineering, Washington University in St. Louis , St. Louis, Missouri 63110, United States.ORCID http://orcid.org/0000-0003-1914-4955
Gregory R BowmanDepartment of Biochemistry and Molecular Biophysics, and ‡Center for Biological Systems Engineering, Washington University in St. Louis , St. Louis, Missouri 63110, United States.
Washington University in St. Louis · US

Funding

MSMs, adaptive sampling, and data sharing on the cloudR01GM124007 · NIGMS · WASHINGTON UNIVERSITY · PI BOWMAN, GREGORY · 2017 to 2021
$2.0M
NIGMS NIH HHS R01 GM124007
6 · The paper itself

Abstract

Allosteric (i.e., long-range) communication within proteins is crucial for many biological processes, such as the activation of signaling cascades in response to specific stimuli. However, the physical basis for this communication remains unclear. Existing computational methods for identifying allostery focus on the role of concerted structural changes, but recent experimental work demonstrates that disorder is also an important factor. Here, we introduce the Correlation of All Rotameric and Dynamical States (CARDS) framework for quantifying correlations between both the structure and disorder of different regions of a protein. To quantify disorder, we draw inspiration from methods for quantifying "dynamic heterogeneity" from chemical physics to classify segments of a dihedral's time evolution as being in either ordered or disordered regimes. To demonstrate the utility of this approach, we apply CARDS to the Catabolite Activator Protein (CAP), a transcriptional activator that is regulated by Cyclic Adenosine MonoPhosphate (cAMP) binding. We find that CARDS captures allosteric communication between the two cAMP-Binding Domains (CBDs). Importantly, CARDS reveals that this coupling is dominated by disorder-mediated correlations, consistent with NMR experiments that establish allosteric coupling between the CBDs occurs without a concerted structural change. CARDS also recapitulates an enhanced role for disorder in the communication between the DNA-Binding Domains (DBDs) and CBDs in the S62F variant of CAP. Finally, we demonstrate that using CARDS to find communication hotspots identifies regions of CAP that are in allosteric communication without foreknowledge of their identities. Therefore, we expect CARDS to be of great utility for both understanding and predicting allostery.

Indexed as

Molecular Dynamics SimulationAllosteric RegulationCyclic AMPDNAMolecular StructureProteinsCyclic AMPDNAProteins

Identifiers

PMID28282132
PMCPMC5934993
OpenAlexW2591912476

What OpenQuestion holds

Textmetadata
LicenceTDM
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.