ArticleJournal of chemical information and modeling2026
Loop Plasticity Drives Paralog-Specific Recognition in BET ET Domains.
Article in Journal of chemical information and modeling, 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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1 citing paper in PubMed.
- Allosteric Protein Chemical Shift Perturbations are Ubiquitous.bioRxiv : the preprint server for biology · 2026Article
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6 authors.
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Abstract
The bromodomain and extraterminal domain (BET) family uses its conserved ET domains to recognize diverse peptide motifs, yet exhibits paralog-specific binding preferences whose structural origins remain poorly understood. Using extensive molecular dynamics (MD) simulations of BRD3-ET and BRD4-ET and experimental data for the unbound and peptide-bound states, we show that paralog selectivity arises not from large structural rearrangements but from subtle differences in the dynamics of the α2-α3 loop. Two divergent residues at positions 35 and 36 in this loop modulate the formation of flanking helices (η1 and η2), which in turn control the opening of the peptide-binding cavity and determine how each paralog accommodates distinct binding modes. These sequence-encoded dynamical differences shape the number, stability, and geometry of accessible binding modes and provide a structural rationale for paralog-specific targeting of BET proteins.
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