A folding-after-binding mechanism describes the recognition between the transactivation domain of c-Myb and the KIX domain of the CREB-binding protein.

No abstract is available for this paper.

• Publication year

  2012

• Venue

  Biochemical and Biophysical Research Communications - BBRC

• Publication date

  2012-11-16

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/j.bbrc.2012.09.112PMID 23026051
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Dynamics and mechanisms of coupled protein folding and binding reactions.

  2012cited by this paper
• Fast Association and Slow Transitions in the Interaction between Two Intrinsically Disordered Protein Domains*

  2012cited by this paper
• Structures of KIX domain of CBP in complex with two FOXO3a transactivation domains reveal promiscuity and plasticity in coactivator recruitment

  2012cited by this paper
• Unstructural biology coming of age.

  2011cited by this paper
• Understanding protein non-folding.

  2010cited by this paper
• Mapping the interactions of the p53 transactivation domain with the KIX domain of CBP.

  2009cited by this paper
• Function and structure of inherently disordered proteins.

  2008cited by this paper
• Selected‐fit versus induced‐fit protein binding: Kinetic differences and mutational analysis

  2008cited by this paper
• Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions.

  2008cited by this paper
• Mechanism of induced folding: Both folding before binding and binding before folding can be realized in staphylococcal nuclease mutants

  2008cited by this paper
• Kinetics of folding and binding of an intrinsically disordered protein: the inhibitor of yeast aspartic proteinase YPrA.

  2008cited by this paper
• Mechanism of coupled folding and binding of an intrinsically disordered protein

  2007cited by this paper
• The interplay between structure and function in intrinsically unstructured proteins

  2005cited by this paper
• Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb.

  2004influential reference
• Cooperativity in Transcription Factor Binding to the Coactivator CREB-binding Protein (CBP)

  2002cited by this paper
• Coupling of folding and binding for unstructured proteins.

  2002cited by this paper
• Speeding molecular recognition by using the folding funnel: the fly-casting mechanism.

  2000cited by this paper
• Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.

  1999cited by this paper
• Trifluoroethanol effects on helix propensity and electrostatic interactions in the helical peptide from ribonuclease T1

  1998cited by this paper
• Structure and mechanism in protein science

  1998cited by this paper
• Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions.

  1997cited by this paper
• Quantitative determination of helical propensities from trifluoroethanol titration curves.

  1994cited by this paper
• Coupling of local folding to site-specific binding of proteins to DNA.

  1994cited by this paper
• The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding.

  1992cited by this paper
• Structure and mechanism

  1989cited by this paper
• Hemoglobin and Myoglobin in Their Reactions with Ligands. Eraldo Antonini and Maurizio Brunori. North-Holland, Amsterdam, 1971 (U.S. distributor, Elsevier, New York). xx, 436 pp., illus. $30. Frontiers of Biology, vol. 21

  1972cited by this paper
• Comparison of experimental binding data and theoretical models in proteins containing subunits.

  1966cited by this paper
• ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

  1965cited by this paper
• Parameters for the Description of Transition States.

  1953cited by this paper

• High-throughput affinity measurements of direct interactions between activation domains and co-activators

  2024cites this paper
• Stereochemistry in the disorder–order continuum of protein interactions

  2024cites this paper
• The transition state for coupled folding and binding of a disordered DNA binding domain resembles the unbound state

  2024cites this paper
• Evolutionary fine-tuning of residual helix structure in disordered proteins manifests in complex structure and lifetime

  2023cites this paper
• Unraveling the Behavior of Intrinsically Disordered Protein c-Myc: A Study Utilizing Gaussian-Accelerated Molecular Dynamics

  2023cites this paper
• The molecular basis for cellular function of intrinsically disordered protein regions

  2023cites this paper
• Binding-and-Folding Recognition of an Intrinsically Disordered Protein Using Online Learning Molecular Dynamics

  2023cites this paper
• Temperature-Jump Spectroscopy of Gold–Poly(N-isopropylacrylamide) Core–Shell Microgels

  2022cites this paper
• Unveiling induced folding of intrinsically disordered proteins - Protein engineering, frustration and emerging themes.

  2021cites this paper
• Japanese encephalitis virus – exploring the dark proteome and disorder–function paradigm

  2020cites this paper
• Conformational dynamics of p53 N-terminal TAD2 region under different solvent conditions.

  2020cites this paper
• Unstructured Biology of Proteins from Ubiquitin-Proteasome System: Roles in Cancer and Neurodegenerative Diseases

  2020cites this paper
• Charge Interactions Modulate the Encounter Complex Ensemble of Two Differently Charged Disordered Protein Partners of KIX.

  2020cites this paper
• Templated folding of intrinsically disordered proteins

  2020cites this paper
• A disordered encounter complex is central to the yeast Abp1p SH3 domain binding pathway

  2020cites this paper
• Folding and structural polymorphism of p53 C-terminal domain: One peptide with many conformations.

  2020cites this paper
• Intrinsically disordered protein domains in flavivirus infection.

  2020cites this paper
• Investigating into the molecular interactions of flavonoids targeting NS2B-NS3 protease from ZIKA virus through in-silico approaches

  2020cites this paper
• The dark side of Alzheimer’s disease: unstructured biology of proteins from the amyloid cascade signaling pathway

  2020cites this paper
• The interaction strength of an intrinsically disordered protein domain with its binding partner is little affected by very different cosolutes.

  2020cites this paper
• Zika virus NS4A cytosolic region (residues 1-48) is an intrinsically disordered domain and folds upon binding to lipids.

  2020cites this paper
• Small molecule inhibitors possibly targeting the rearrangement of Zika virus Envelope protein.

  2020cites this paper
• Measuring and Analyzing Binding Kinetics of Coupled Folding and Binding Reactions Under Pseudo-First-Order Conditions.

  2020cites this paper
• Consideration of Binding Kinetics in the Design of Stapled Peptide Mimics of the Disordered Proteins Eukaryotic Translation Initiation Factor 4E-Binding Protein 1 and Eukaryotic Translation Initiation Factor 4G.

  2019cites this paper
• The dark proteome of cancer: Intrinsic disorderedness and functionality of HIF-1α along with its interacting proteins.

  2019cites this paper
• Structural and mechanistic insights into the interaction of the circadian transcription factor BMAL1 with the KIX domain of the CREB-binding protein

  2019cites this paper
• Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding

  2019cites this paper
• Binding induced folding: Lessons from the kinetics of interaction between NTAIL and XD.

  2019cites this paper
• Mechanistic Insights into Zika Virus NS3 Helicase Inhibition by Epigallocatechin-3-Gallate

  2019cites this paper
• Experimental studies of binding of intrinsically disordered proteins to their partners

  2019cites this paper
• Inhibits Zika Virus NS 2 BNS 3 Protease

  2019cites this paper
• Folding perspectives of an intrinsically disordered transactivation domain and its single mutation breaking the folding propensity.

  2019cites this paper
• Understanding the interactability of chikungunya virus proteins via molecular recognition feature analysis

  2018cites this paper
• E7 oncoprotein of human papillomavirus: Structural dynamics and inhibitor screening study.

  2018cites this paper
• Conservation of coactivator engagement mechanism enables small-molecule allosteric modulators

  2018cites this paper
• Stopped-Flow Kinetic Techniques for Studying Binding Reactions of Intrinsically Disordered Proteins.

  2018cites this paper
• Hydroxychloroquine Inhibits Zika Virus NS2B-NS3 Protease

  2018cites this paper
• МЕХАНИЗМ СВОРАЧИВАНИЯ ТРАНСАКТИВАЦИОННОГО ДОМЕНА Е-БЕЛКОВ ПРИ ВЗАИМОДЕЙСТВИИ С KIX-ДОМЕНОМ КОАКТИВАТОРА ТРАНСКРИПЦИИ CBP, "Цитология"

  2018cites this paper
• Molecular Simulations of Pathways and Kinetics for Protein-protein Binding Processes

  2018cites this paper
• Dissecting Transcriptional Coactivator Binding Networks To Enable Small Molecule Modulation

  2017cites this paper
• Eukaryotic transcription factors: paradigms of protein intrinsic disorder.

  2017cites this paper
• The IDP-Specific Force Field ff14IDPSFF Improves the Conformer Sampling of Intrinsically Disordered Proteins

  2017cites this paper
• Flexibility vs Preorganization: Direct Comparison of Binding Kinetics for a Disordered Peptide and Its Exact Preorganized Analogues.

  2017cites this paper
• Therapeutic Interventions of Cancers Using Intrinsically Disordered Proteins as Drug Targets: c-Myc as Model System

  2017cites this paper
• Deciphering the promiscuous interactions between intrinsically disordered transactivation domains and the KIX domain

  2017cites this paper
• Mechanistic roles of protein disorder within transcription.

  2017cites this paper
• Molecular Recognition Features in Zika Virus Proteome.

  2017cites this paper
• pKID Binds to KIX via an Unstructured Transition State with Nonnative Interactions

  2017cites this paper
• Epigallocatechin gallate, an active green tea compound inhibits the Zika virus entry into host cells via binding the envelope protein.

  2017cites this paper
• Discovery of Small Molecules to Dissect the Individual Roles of GACKIX-Activator Complexes

  2017influential citation
• Coupled binding and folding of intrinsically disordered proteins: what can we learn from kinetics?

  2016cites this paper
• Modulation Of Circadian Cycling By The C-Terminal Transactivation Domain Of BMAL1

  2016cites this paper
• Molecular Determinants of Tubulin's C-Terminal Tail Conformational Ensemble.

  2016cites this paper
• Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300*

  2016cites this paper
• Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies*

  2016cites this paper
• Structured and Unstructured Binding of an Intrinsically Disordered Protein as Revealed by Atomistic Simulations.

  2016cites this paper
• Molecular Dynamics of the disordered γ-tubulin carboxyl terminus

  2016influential citation
• Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein

  2016cites this paper
• Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment

  2016influential citation
• Intrinsically Disordered Side of the Zika Virus Proteome

  2016cites this paper
• Demonstration of a folding after binding mechanism in the recognition between the measles virus NTAIL and X domains.

  2015cites this paper
• Binding Rate Constants Reveal Distinct Features of Disordered Protein Domains.

  2015cites this paper
• Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding

  2015cites this paper
• Shared structural features of the 9aaTAD family in complex with CBP.

  2015cites this paper
• Functional advantages of dynamic protein disorder

  2015cites this paper
• Ethanol Activation of PKA Mediates Single-Minded 2 Expression in Neuronal Cells

  2014cites this paper
• Intrinsically disordered proteins in cellular signalling and regulation

  2014cites this paper
• Prepaying the entropic cost for allosteric regulation in KIX

  2014cites this paper
• A Frustrated Binding Interface for Intrinsically Disordered Proteins*

  2014cites this paper
• The mechanism of binding of the KIX domain to the mixed lineage leukemia protein and its allosteric role in the recognition of c‐Myb

  2014cites this paper
• Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants

  2014cites this paper
• The binding mechanisms of intrinsically disordered proteins.

  2014cites this paper
• Deciphering the mechanisms of binding induced folding at nearly atomic resolution: The Φ value analysis applied to IDPs

  2014cites this paper
• Structure of the transition state for the binding of c-Myb and KIX highlights an unexpected order for a disordered system

  2013cites this paper
• MORPHOGENESIS OF PROTEINS: CLASSIC VIEWS AND CHALLENGES AHEAD

  2013cites this paper
• Molecular recognition by the KIX domain and its role in gene regulation

  2013cites this paper
• Remarkably Fast Coupled Folding and Binding of the Intrinsically Disordered Transactivation Domain of cMyb to CBP KIX

  2013cites this paper
• The transition state structure for coupled binding and folding of disordered protein domains

  2013cites this paper
• Kinetic and Conformational Characterization of Transcriptional Activator-Coactivator Interactions.

  2013cites this paper