Evidence map›Paper›PMID 23651431›Full record

ArticleACS chemical biology2013

Allosteric communication in the KIX domain proceeds through dynamic repacking of the hydrophobic core.

Sven Brüschweiler, Robert Konrat, Martin Tollinger

Abstract read
In one paragraph

Article in ACS chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Article
  2. CBP/p300, a promising therapeutic target for prostate cancer.Journal of translational medicine · 2025
    Review
  3. Article
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  5. Fluorine-Thiol Displacement Stapling on the Disordered αSynlett : accounts and rapid communications in synthetic organic chemistry · 2025
    Article
  6. Article
  7. Assessing the applicability ofJournal of biomolecular NMR · 2023
    Article
  8. Article
  9. Peptide-based covalent inhibitors of protein-protein interactions.Journal of peptide science : an official publication of the European Peptide Society · 2023
    Review
  10. iScience · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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.

Sven BrüschweilerInstitute of Organic Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck , Innrain 80/82, A-6020 Innsbruck, Austria.
Robert Konrat
Martin Tollinger

Funding

Austrian Science Fund FWF P 22735
6 · The paper itself

Abstract

The KIX domain of the transcriptional coactivator CREB binding protein (CBP) co-operatively mediates interactions between transcription factors. Binding of the transcription factor mixed-lineage leukemia (MLL) induces the formation of a low-populated conformer of KIX that resembles the conformation of the KIX domain in the presence of a second transcription factor molecule. NMR spin relaxation studies have previously shown that allosteric coupling proceeds through a network of hydrophobic core residues that bridge the two binding sites. Here we describe high-resolution NMR solution structures of the binary complex of KIX with MLL and the ternary complex of KIX formed with MLL and phosphorylated kinase inducible domain of CREB (pKID) as a second ligand. We show that binding of pKID to the binary complex of KIX with MLL is accompanied by a defined repacking of the allosteric network in the hydrophobic core of the protein. Rotamer populations derived from methyl group (13)C chemical shifts reveal a dynamic contribution to the repacking process that is not captured by the structural coordinates and exemplify the dynamic nature of allosteric communication in the KIX domain.

Indexed as

Protein Structure, TertiaryAllosteric RegulationCoordination ComplexesCREB-Binding ProteinHydrophobic and Hydrophilic InteractionsMagnetic Resonance SpectroscopyModels, BiologicalMolecular ConformationCoordination ComplexesCREB-Binding Protein

Identifiers

PMID23651431
PMCPMC3719477

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.