ArticleBiophysical journal2016
Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- How intrinsically disordered regions shape the function of CREB-binding protein.Biochemical Society transactions · 2026Review
- CBP-IDRs regulate acetylation and gene expression.Cell reports · 2026Article
- Decoding Order and Disorder in Proteins by NMR Spectroscopy.Journal of the American Chemical Society · 2025Article
- Unraveling the Tether: Exploring Representative Protein Linkers and Their Structural and Thermodynamical Properties.The journal of physical chemistry. B · 2025Article
- Article
- Predicting the sequence-dependent backbone dynamics of intrinsically disordered proteins.eLife · 2024Article
- Predicting the Sequence-Dependent Backbone Dynamics of Intrinsically Disordered Proteins.bioRxiv : the preprint server for biology · 2024Article
- Protein ensemble modeling and analysis with MMMx.Protein science : a publication of the Protein Society · 2024Article
- Chemistry towards Biology-Instruct: Snapshot.International journal of molecular sciences · 2022Review
- Review
- A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins.Structure (London, England : 1993) · 2021Article
- Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues.Magnetic resonance (Gottingen, Germany) · 2021Article
- Article
- Interaction between the scaffold proteins CBP by IQGAP1 provides an interface between gene expression and cytoskeletal activity.Scientific reports · 2020Article
- Taking Simultaneous Snapshots of Intrinsically Disordered Proteins in Action.Biophysical journal · 2019Article
- PreSMo Target-Binding Signatures in Intrinsically Disordered Proteins.Molecules and cells · 2018Review
- An efficient combination of BEST and NUS methods in multidimensional NMR spectroscopy for high throughput analysis of proteins.RSC advances · 2018Article
- Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP.Scientific reports · 2017Article
- Reconstruction of non-uniformly sampled five-dimensional NMR spectra by signal separation algorithm.Journal of biomolecular NMR · 2017Article
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Authors and funding
8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Here, we present a structural and dynamic description of CBP-ID4 at atomic resolution. ID4 is the fourth intrinsically disordered linker of CREB-binding protein (CBP). In spite of the largely disordered nature of CBP-ID4, NMR chemical shifts and relaxation measurements show a significant degree of α-helix sampling in the protein regions encompassing residues 2-25 and 101-128 (1852-1875 and 1951-1978 in full-length CBP). Proline residues are uniformly distributed along the polypeptide, except for the two α-helical regions, indicating that they play an active role in modulating the structural features of this CBP fragment. The two helical regions are lacking known functional motifs, suggesting that they represent thus-far uncharacterized functional modules of CBP. This work provides insights into the functions of this protein linker that may exploit its plasticity to modulate the relative orientations of neighboring folded domains of CBP and fine-tune its interactions with a multitude of partners.
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