ArticleBiochemistry2014
Binding hotspots of BAZ2B bromodomain: Histone interaction revealed by solution NMR driven docking.
Article in Biochemistry, 2014. 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.
- Pan-cancer and multi-omics analyses reveal the diagnostic and prognostic value of BAZ2B in cancer.Scientific reports · 2026Article
- Biochemical and cellular insights into the Baz2B protein, a non-catalytic subunit of the chromatin remodeling complex.Nucleic acids research · 2024Article
- The role of loop dynamics in the prediction of ligand-protein binding enthalpy.Chemical science · 2023Article
- Unusual pBiomacromolecules · 2023Article
- Crystal structure of the BAZ2B TAM domain.Heliyon · 2022Article
- NMR Molecular Replacement Provides New Insights into Binding Modes to Bromodomains of BRD4 and TRIM24.Journal of medicinal chemistry · 2022Article
- Targeting TRIM Proteins: A Quest towards Drugging an Emerging Protein Class.Chembiochem : a European journal of chemical biology · 2021Review
- Article
- Discovery of a hidden transient state in all bromodomain families.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Small Molecules Targeting the Specific Domains of Histone-Mark Readers in Cancer Therapy.Molecules (Basel, Switzerland) · 2020Review
- DNA binding drives the association of BRG1/hBRM bromodomains with nucleosomes.Nature communications · 2017Article
- Structural basis of molecular recognition of helical histone H3 tail by PHD finger domains.The Biochemical journal · 2017Article
- Protein dynamics and structural waters in bromodomains.PloS one · 2017Article
- Dual Screening of BPTF and Brd4 Using Protein-Observed Fluorine NMR Uncovers New Bromodomain Probe Molecules.ACS chemical biology · 2015Article
- WONKA: objective novel complex analysis for ensembles of protein-ligand structures.Journal of computer-aided molecular design · 2015Article
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Authors and funding
8 authors.
Funding
Abstract
Bromodomains are epigenetic reader domains, which have come under increasing scrutiny both from academic and pharmaceutical research groups. Effective targeting of the BAZ2B bromodomain by small molecule inhibitors has been recently reported, but no structural information is yet available on the interaction with its natural binding partner, acetylated histone H3K14ac. We have assigned the BAZ2B bromodomain and studied its interaction with H3K14ac acetylated peptides by NMR spectroscopy using both chemical shift perturbation (CSP) data and clean chemical exchange (CLEANEX-PM) NMR experiments. The latter was used to characterize water molecules known to play an important role in mediating interactions. Besides the anticipated Kac binding site, we consistently found the bromodomain BC loop as hotspots for the interaction. This information was used to create a data-driven model for the complex using HADDOCK. Our findings provide both structure and dynamics characterization that will be useful in the quest for potent and selective inhibitors to probe the function of the BAZ2B bromodomain.
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