ArticleProtein science : a publication of the Protein Society2020
Structure of the BRK domain of the SWI/SNF chromatin remodeling complex subunit BRG1 reveals a potential role in protein-protein interactions.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 21 citations in OpenAlex.
- Osimertinib Resistance in EGFR-Mutated Non-Small Cell Lung Cancer: Mechanisms and Therapeutic Strategies.MedComm · 2026Review
- Single-molecule imaging of SWI/SNF chromatin remodelers reveals bromodomain-mediated and cancer-mutants-specific landscape of multi-modal DNA-binding dynamics.Nature communications · 2024Article
- Transcriptional and spatiotemporal regulation of the dauer program.Transcription · 2023Review
- The effect of a single SMARCA4 exon deletion on RNA splicing: Implications for variant classification.Molecular genetics & genomic medicine · 2023Article
- Review
- Nuclear Actin Dynamics in Gene Expression, DNA Repair, and Cancer.Results and problems in cell differentiation · 2022Article
- Paralog Explorer: A resource for mining information about paralogs in common research organisms.Computational and structural biotechnology journal · 2022Article
- HERVH-derived lncRNAs negatively regulate chromatin targeting and remodeling mediated by CHD7.Life science alliance · 2022Article
- Exploiting vulnerabilities of SWI/SNF chromatin remodelling complexes for cancer therapy.Oncogene · 2021Review
- Exploring the Interaction between the SWI/SNF Chromatin Remodeling Complex and the Zinc Finger Factor CTCF.International journal of molecular sciences · 2020Article
- The structural biology of canonical Wnt signalling.Biochemical Society transactions · 2020Review
- Non-Coding RNAs and Nucleosome Remodeling Complexes: An Intricate Regulatory Relationship.Biology · 2020Review
- Structure of the BRK domain of the SWI/SNF chromatin remodeling complex subunit BRG1 reveals a potential role in protein-protein interactions.Protein science : a publication of the Protein Society · 2020Article
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3 authors at 2 institutions in 2 countries.
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Abstract
BRG1/SMARCA4 and its paralog BRM/SMARCA2 are the ATPase subunits of human SWI/SNF chromatin remodeling complexes. These multisubunit assemblies can act as either tumor suppressors or drivers of cancer, and inhibiting both BRG1 and BRM, is emerging as an effective therapeutic strategy in diverse cancers. BRG1 and BRM contain a BRK domain. The function of this domain is unknown, but it is often found in proteins involved in transcription and developmental signaling in higher eukaryotes, in particular in proteins that remodel chromatin. We report the NMR structure of the BRG1 BRK domain. It shows similarity to the glycine-tyrosine-phenylalanine (GYF) domain, an established protein-protein interaction module. Computational peptide-binding-site analysis of the BRK domain identifies a binding site that coincides with a highly conserved groove on the surface of the protein. This sets the scene for experiments to elucidate the role of this domain, and evaluate the potential of targeting it for cancer therapy.
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