ArticleNature communications2026
Allosteric and energetic remodeling of a PDZ domain by protein domain extensions.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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.
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.
Who cites it
4 citing papers in PubMed.
- Decoding the allosteric grammar of protein kinases: A dual-stream framework integrating protein language models and energy landscape frustration analysis.Protein science : a publication of the Protein Society · 2026Article
- Amplicon/Protein Bead Display enables quantitativebioRxiv : the preprint server for biology · 2026Article
- Predicting and Decoding Allosteric Binding Sites Using Protein Language Models and Structure-Based Machine Learning: An Energy Landscape-Guided Explainable AI Framework.Journal of chemical theory and computation · 2026Article
- Seven complete comparative maps of allosteric mutations in a protein family.Nature communications · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Many functions of proteins are performed by independently folding structural units called domains. These domains are structurally conserved but not identical in different proteins. Here, to understand the consequences for regulation and evolvability of domain extensions, we quantify the energetic effects of two extensions in a model protein domain. Quantifying abundance and ligand binding for >190,000 protein variants allows us to measure the free energy changes for mutations throughout a PDZ domain and ~7000 energetic couplings between these mutations and two domain extensions. Both a structured extension and a more dynamic extension substantially but specifically re-shape the energy landscape. In particular, deleting an ɑ-helix alters the energetic consequences of >400 mutations in >50 sites on fold stability or binding energy, and the effects of >300 allosteric mutations, including at solvent-accessible surface sites. Extending or pruning the domain therefore reshapes its energetic and allosteric landscape, adding and removing opportunities for the allosteric control of protein function.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.