ArticleBiophysical journal2012
Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- Distinct Molten-Globule Conformations in an Interacting Protein Domain Resolved byAngewandte Chemie (International ed. in English) · 2026Article
- Elevated conformational dynamics makes ACKR3 activation-prone and G protein-incompetent.bioRxiv : the preprint server for biology · 2026Article
- Intrinsically Disordered Flanking Regions Increase the Affinity of a Transcriptional Coactivator Interaction across Vertebrates.Biochemistry · 2023Article
- Amino acid motifs for the identification of novel protein interactants.Computational and structural biotechnology journal · 2023Review
- The dynamic properties of a nuclear coactivator binding domain are evolutionarily conserved.Communications biology · 2022Article
- Coupled Binding and Helix Formation Monitored by Synchrotron-Radiation Circular Dichroism.Biophysical journal · 2019Article
- Article
- The Differential Response of Proteins to Macromolecular Crowding.PLoS computational biology · 2016Article
- Expanding the Range of Protein Function at the Far End of the Order-Structure Continuum.The Journal of biological chemistry · 2016Review
- The transition state structure for coupled binding and folding of disordered protein domains.Scientific reports · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear coactivator binding domain of CREB binding protein folds into remarkably different structures in complex with different ligands. To understand the mechanism of the structural adaptability in the nuclear coactivator binding domain (NCBD), we have compared the dynamics of the hydrophobic core of NCBD in the ligand-free state and in a well-folded complex with the ligand activator for thyroid hormone and retinoid receptors using multiple NMR methods including methyl chemical shifts, coupling constants, and methyl order parameters. From all NMR measures, the aliphatic side chains in the hydrophobic core are slightly more dynamic in the free protein than in the complex, but have mobility comparable to the hydrophobic cores of average folded proteins. Urea titration monitored by NMR reveals that all parts of the protein, including the side-chain packing in the hydrophobic core, denatures in a single cooperative process. The molten globule characteristics of NCBD are thus restricted to a slowly fluctuating tertiary structure. Consequently, the conformational plasticity of the protein is most likely related to its low overall stability rather than an intrinsically flexible protein structure. The well-defined structure supports a model of molecular recognition dominated by conformational selection, whereas only minor structural adjustments are necessary after the association.
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