ArticleJournal of molecular biology2018
Uncoupling the Folding and Binding of an Intrinsically Disordered Protein.
Article in Journal of molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Alternative Splicing of a Structured Partner Alters the Folding-Upon-Binding Trajectory of an Intrinsically Disordered Protein.Journal of the American Chemical Society · 2026Article
- Disordered but rhythmic-the role of intrinsic protein disorder in eukaryotic circadian timing.FEBS letters · 2026Review
- Cooperative multivalency converts disorder into rods, resolving a paradox in cellular architecture.bioRxiv : the preprint server for biology · 2026Article
- Role of charges in a dynamic disordered complex between an IDP and a folded domain.Nature communications · 2025Article
- Fibrinogen-binding M-related proteins facilitate the recruitment of plasminogen by Streptococcus pyogenes.Protein science : a publication of the Protein Society · 2025Article
- High-throughput affinity measurements of direct interactions between activation domains and co-activators.bioRxiv : the preprint server for biology · 2024Article
- Binding-and-Folding Recognition of an Intrinsically Disordered Protein Using Online Learning Molecular Dynamics.Journal of chemical theory and computation · 2023Article
- The free energy folding penalty accompanying binding of intrinsically disordered α-helical motifs.Protein science : a publication of the Protein Society · 2022Article
- Rational design of a helical peptide inhibitor targeting c-Myb-KIX interaction.Scientific reports · 2022Article
- The sequence-ensemble relationship in fuzzy protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Calcium Solubilization Ability and Anti-Inflammatory Effects of Hydrolyzed Casein.Food science of animal resources · 2021Article
- A disordered encounter complex is central to the yeast Abp1p SH3 domain binding pathway.PLoS computational biology · 2020Article
- Disorder for Dummies: Functional Mutagenesis of Transient Helical Segments in Disordered Proteins.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Intrinsically Disordered Proteins: Structure, Function and Therapeutics.Journal of molecular biology · 2018Article
- Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins.Methods in enzymology · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The relationship between helical stability and binding affinity was examined for the intrinsically disordered transactivation domain of the myeloblastosis oncoprotein, c-Myb, and its ordered binding partner, KIX. A series of c-Myb mutants was designed to either increase or decrease helical stability without changing the binding interface with KIX. This included a complimentary series of A, G, P, and V mutants at three non-interacting sites. We were able to use the glycine mutants as a reference state and show a strong correlation between binding affinity and helical stability. The intrinsic helicity of c-Myb is 21%, and helicity values of the mutants ranged from 8% to 28%. The c-Myb helix is divided into two conformationally distinct segments. The N-terminal segment, from K291-L301, has an average helicity greater than 60% and the C-terminal segment, from S304-L315, has an average helicity less than 10%. We observed different effects on binding when these two segments were mutated. Mutants in the N-terminal segment that increased helicity had no effect on the binding affinity to KIX, while helix destabilizing glycine and proline mutants reduced binding affinity by more than 1 kcal/mol. Mutants that either increased or decreased helical stability in the C-terminal segment had almost no effect on binding. However, several of the mutants reveal the presence of multiple conformations accessible in the bound state based on changes in enthalpy and linkage analysis of binding free energies. These results may explain the high level of sequence identity (>90%), even at non-interacting sites, for c-Myb homologues.
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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.