Evidence map›Paper›PMID 19841628›Full record

ReviewNature chemical biology2009

The role of dynamic conformational ensembles in biomolecular recognition.

David D Boehr, Ruth Nussinov, Peter E Wright

Erratum issuedAbstract readReview
In one paragraph

Review in Nature chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 882 papers.

0numbers the graph read from it
0cells of the map it votes in
882citing 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

882 citing papers in PubMed.

  1. Single-Molecule Force Spectroscopy: Experiments, Analysis, and Simulations.Methods in molecular biology (Clifton, N.J.) · 2027
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  19. Crystal structure of human Dickkopf 4 cysteine-rich domain 1 and evaluation of conformational rigidity.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  20. Article

822 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors.

David D BoehrDepartment of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, USA. ddb12@psu.edu
Ruth Nussinov
Peter E Wright

Funding

Protein Structure, Stability, and Amyloid FormationZIABC010440 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$11.8M
Biomolecular Recognition and Binding MechanismsZIABC010441 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$9.4M
Structural basis for CBP/p300 transcriptional regulationR01CA096865 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI WRIGHT, PETER EDWIN · 2002 to 2016
$6.2M
Protein Dynamics in Dihydrofolate Reductase CatalysisR01GM075995 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WRIGHT, PETER EDWIN · 2006 to 2021
$6.1M
Intramural NIH HHSNCI NIH HHS CA96865NCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400NCI NIH HHS R01 CA096865NIGMS NIH HHS GM75995NIGMS NIH HHS R01 GM075995
6 · The paper itself

Abstract

Molecular recognition is central to all biological processes. For the past 50 years, Koshland's 'induced fit' hypothesis has been the textbook explanation for molecular recognition events. However, recent experimental evidence supports an alternative mechanism. 'Conformational selection' postulates that all protein conformations pre-exist, and the ligand selects the most favored conformation. Following binding the ensemble undergoes a population shift, redistributing the conformational states. Both conformational selection and induced fit appear to play roles. Following binding by a primary conformational selection event, optimization of side chain and backbone interactions is likely to proceed by an induced fit mechanism. Conformational selection has been observed for protein-ligand, protein-protein, protein-DNA, protein-RNA and RNA-ligand interactions. These data support a new molecular recognition paradigm for processes as diverse as signaling, catalysis, gene regulation and protein aggregation in disease, which has the potential to significantly impact our views and strategies in drug design, biomolecular engineering and molecular evolution.

Indexed as

Molecular ConformationBinding SitesDatabases, ProteinDiseaseDNADrug DesignEnzymesEvolution, MolecularGene Expression RegulationGenetic EngineeringHumansLigandsModels, MolecularPattern Recognition, VisualProtein ConformationProteinsDNAEnzymesLigandsProteinsRepressor ProteinsRNA

Identifiers

PMID19841628
PMCPMC2916928

What OpenQuestion holds

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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.