ArticleProtein science : a publication of the Protein Society2026
Sequence-encoded dynamics diversify allostery within a conserved protein scaffold.
Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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.
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Who cites it
1 citing paper in PubMed.
- Sequence-encoded dynamics diversify allostery within a conserved protein scaffold.Protein science : a publication of the Protein Society · 2026Article
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Authors and funding
5 authors.
Funding
Abstract
Proteins evolve allosteric mechanisms through sequence variation while preserving a conserved structural fold. How these substitutions reshape the protein's conformational landscape to drive functional diversification remains poorly understood. Members of the cAMP receptor protein family (CRP), a ubiquitous bacterial transcription factor, share a common architecture yet differentially couple cAMP binding to DNA interactions. Here, our results support a model in which allosteric diversification in CRP arises from the tuning of sequence-encoded protein's conformational dynamics. Comparative analysis of sequence conservation and helical propensity across proteobacterial and actinobacterial CRPs reveals lineage-specific distributions of conformational heterogeneity within the dimerization C-helix. These evolutionary patterns map onto the proteobacterial Escherichia coli (E. coli) CRP and the actinobacterial Mycobacterium tuberculosis (MTB) CRP, two protein homologs that respond to cAMP through distinct allosteric mechanisms. Guided by functional and evolutionary differences, we introduced CRP
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