ArticleProceedings of the National Academy of Sciences of the United States of America2020
Supertertiary protein structure affects an allosteric network.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
- Interpretable biophysical neural networks of transcriptional activation domains separate roles of protein abundance and coactivator binding.Cell systems · 2026Article
- Allosteric and energetic remodeling of a PDZ domain by protein domain extensions.Nature communications · 2026Article
- Robust SH2 binding affinity indicates minimal SH3-to-SH2 communication in Grb2.Biology direct · 2026Article
- Dissecting the Structural Features of Folding Asymmetry and Transient Misfolding in a Multidomain PDZ Scaffold.Small science · 2026Article
- Allosteric modulation of Grb2 drives ligand-dependent signal responses.Biology direct · 2025Article
- Exploring Innovative Approaches to Isolate a One-Component c-di-GMP Transducer: A Pilot Study.Advances in experimental medicine and biology · 2025Article
- MoCHI: neural networks to fit interpretable models and quantify energies, energetic couplings, epistasis, and allostery from deep mutational scanning data.Genome biology · 2024Article
- A PDZ tandem repeat folds and unfolds via different pathways.Protein science : a publication of the Protein Society · 2024Article
- Conservation of Affinity Rather Than Sequence Underlies a Dynamic Evolution of the Motif-Mediated p53/MDM2 Interaction in Ray-Finned Fishes.Molecular biology and evolution · 2024Article
- Addressing the Binding Mechanism of the Meprin and TRAF-C Homology Domain of the Speckle-Type POZ Protein Using Protein Engineering.International journal of molecular sciences · 2023Article
- Membrane recruitment of the polarity protein Scribble by the cell adhesion receptor TMIGD1.Communications biology · 2023Article
- Viral subversion of the cell polarity regulator Scribble.Biochemical Society transactions · 2023Review
- Determinants of affinity, specificity, and phase separation in a supramodule from Post-synaptic density protein 95.iScience · 2022Article
- Molecular basis of Tick Born encephalitis virus NS5 mediated subversion of apico-basal cell polarity signalling.The Biochemical journal · 2022Article
- Article
- Structural and dynamic studies of the peptidase domain from Clostridium thermocellum PCAT1.Protein science : a publication of the Protein Society · 2022Article
- On the Effects of Disordered Tails, Supertertiary Structure and Quinary Interactions on the Folding and Function of Protein Domains.Biomolecules · 2022Review
- Allosteric regulation of GRB2 modulates RAS activation.Small GTPases · 2022Article
- Exosite binding modulates the specificity of the immunomodulatory enzyme ScpA, a C5a inactivating bacterial protease.Computational and structural biotechnology journal · 2022Article
- Molecular Dynamics-Based Allosteric Prediction Method to Design Key Residues in Threonine Dehydrogenase for Amino-Acid Production.ACS omega · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The notion that protein function is allosterically regulated by structural or dynamic changes in proteins has been extensively investigated in several protein domains in isolation. In particular, PDZ domains have represented a paradigm for these studies, despite providing conflicting results. Furthermore, it is still unknown how the association between protein domains in supramodules, consitituting so-called supertertiary structures, affects allosteric networks. Here, we experimentally mapped the allosteric network in a PDZ:ligand complex, both in isolation and in the context of a supramodular structure, and show that allosteric networks in a PDZ domain are highly dependent on the supertertiary structure in which they are present. This striking sensitivity of allosteric networks to the presence of adjacent protein domains is likely a common property of supertertiary structures in proteins. Our findings have general implications for prediction of allosteric networks from primary and tertiary structures and for quantitative descriptions of allostery.
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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.