ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structure of the transition state for the binding of c-Myb and KIX highlights an unexpected order for a disordered system.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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55 citing papers in PubMed.
- Determinants of Protein Folding Pathways: Lessons from Metamorphic Proteins.International journal of molecular sciences · 2026Review
- Predictive Model for Single-Site Mutations That Change Intrinsically Disordered Protein Binding Energetics.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The transition state for coupled folding and binding of a disordered DNA binding domain resembles the unbound state.Nucleic acids research · 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
- An intramolecular energetic network regulates ligand recognition in a SH2 domain.Protein science : a publication of the Protein Society · 2023Article
- Binding-and-Folding Recognition of an Intrinsically Disordered Protein Using Online Learning Molecular Dynamics.Journal of chemical theory and computation · 2023Article
- Functional regulation of an intrinsically disordered protein via a conformationally excited state.Science advances · 2023Article
- Mutational scan inferred binding energetics and structure in intrinsically disordered protein CcdA.Protein science : a publication of the Protein Society · 2023Article
- Evolutionary fine-tuning of residual helix structure in disordered proteins manifests in complex structure and lifetime.Communications biology · 2023Article
- The Intrinsically Disordered Proteins MLLT3 (AF9) and MLLT1 (ENL) - Multimodal Transcriptional Switches With Roles in Normal Hematopoiesis, MLL Fusion Leukemia, and Kidney Cancer.Journal of molecular biology · 2022Review
- Transactivation domain of Adenovirus Early Region 1A (E1A): Investigating folding dynamics and aggregation.Current research in structural biology · 2022Article
- Prediction of protein-protein interaction sites in intrinsically disordered proteins.Frontiers in molecular biosciences · 2022Review
- Molecular Details of a Coupled Binding and Folding Reaction between the Amyloid Precursor Protein and a Folded Domain.ACS chemical biology · 2021Article
- Fuzziness and Frustration in the Energy Landscape of Protein Folding, Function, and Assembly.Accounts of chemical research · 2021Review
- Understanding the Binding Transition State After the Conformational Selection Step: The Second Half of the Molecular Recognition Process Between NS1 of the 1918 Influenza Virus and Host p85β.Frontiers in molecular biosciences · 2021Article
- Kinetic Methods of Deducing Binding Mechanisms Involving Intrinsically Disordered Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins.The Journal of biological chemistry · 2020Article
- Intrinsically Disordered Bacterial Polar Organizing Protein Z, PopZ, Interacts with Protein Binding Partners Through an N-terminal Molecular Recognition Feature.Journal of molecular biology · 2020Article
- Unexpected specificity within dynamic transcriptional protein-protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The dark side of Alzheimer's disease: unstructured biology of proteins from the amyloid cascade signaling pathway.Cellular and molecular life sciences : CMLS · 2020Article
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5 authors.
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Abstract
A classical dogma of molecular biology dictates that the 3D structure of a protein is necessary for its function. However, a considerable fraction of the human proteome, although functional, does not adopt a defined folded state under physiological conditions. These intrinsically disordered proteins tend to fold upon binding to their partners with a molecular mechanism that is elusive to experimental characterization. Indeed, although many hypotheses have been put forward, the functional role (if any) of disorder in these intrinsically denatured systems is still shrouded in mystery. Here, we characterize the structure of the transition state of the binding-induced folding in the reaction between the KIX domain of the CREB-binding protein and the transactivation domain of c-Myb. The analysis, based on the characterization of a series of conservative site-directed mutants, reveals a very high content of native-like structure in the transition state and indicates that the recognition between KIX and c-Myb is geometrically precise. The implications of our results in the light of previous work on intrinsically unstructured systems are discussed.
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