ArticleProceedings of the National Academy of Sciences of the United States of America2010
Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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76 citing papers in PubMed, 172 citations in OpenAlex.
- Distinct Molten-Globule Conformations in an Interacting Protein Domain Resolved byAngewandte Chemie (International ed. in English) · 2026Article
- Protein rheostasis: quality control in metastable proteomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Transient tertiary structure in intrinsically disordered proteins revealed by multithermal enhanced sampling.Nature communications · 2026Article
- Stability and interaction defects in the Sin3A-PAH1 αα-hub domain associated with loss-of-function variants.The Journal of biological chemistry · 2026Article
- Decoding Order and Disorder in Proteins by NMR Spectroscopy.Journal of the American Chemical Society · 2025Article
- Fine-Tuning of ATF4 DNA Binding Activity by a Secondary Basic Motif Unique to the ATF-X Subfamily of bZip Transcription Factors.Biochemistry · 2025Article
- Inhibition of Aurora-A/N-Myc Protein-Protein Interaction Using Peptidomimetics: Understanding the Role of Peptide Cyclization.Chembiochem : a European journal of chemical biology · 2024Article
- Intrinsically Disordered Flanking Regions Increase the Affinity of a Transcriptional Coactivator Interaction across Vertebrates.Biochemistry · 2023Article
- A look at the face of the molten globule: Structural model of the Helicobacter pylori apoflavodoxin ensemble at acidic pH.Protein science : a publication of the Protein Society · 2022Article
- A modular approach to map out the conformational landscapes of unbound intrinsically disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The dynamic properties of a nuclear coactivator binding domain are evolutionarily conserved.Communications biology · 2022Article
- Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma.Biophysics reviews · 2022Review
- Labeling of Proteins for Single-Molecule Fluorescence Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Advances in targeting 'undruggable' transcription factors with small molecules.Nature reviews. Drug discovery · 2021Review
- Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues.Magnetic resonance (Gottingen, Germany) · 2021Article
- Article
- Conformational editing of intrinsically disordered protein by α-methylation.Chemical science · 2020Article
- High affinity between CREBBP/p300 and NCOA evolved in vertebrates.Protein science : a publication of the Protein Society · 2020Article
- Depletion interactions modulate the binding between disordered proteins in crowded environments.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Investigating the Conformational Ensembles of Intrinsically Disordered Proteins with a Simple Physics-Based Model.The journal of physical chemistry. B · 2020Article
16 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Native molten globules are the most folded kind of intrinsically disordered proteins. Little is known about the mechanism by which native molten globules bind to their cognate ligands to form fully folded complexes. The nuclear coactivator binding domain (NCBD) of CREB binding protein is particularly interesting in this respect as structural studies of its complexes have shown that NCBD folds into two remarkably different states depending on the ligand being ACTR or IRF-3. The ligand-free state of NCBD was characterized in order to understand the mechanism of folding upon ligand binding. Biophysical studies show that despite the molten globule nature of the domain, it contains a small cooperatively folded core. By NMR spectroscopy, we have demonstrated that the folded core of NCBD has a well ordered conformer with specific side chain packing. This conformer resembles the structure of the NCBD in complex with the protein ligand, ACTR, suggesting that ACTR binds to prefolded NCBD molecules from the ensemble of interconverting structures.
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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.