ArticleBiomolecular NMR assignments2025
Resonance assignment of the intrinsically disordered actin-binding region of Drebrin.
Article in Biomolecular NMR assignments, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Structural mechanisms of drebrin-mediated F-actin network modulation.Nature communications · 2026Article
- Diffusion-based size determination of solute particles: a method adapted for postsynaptic proteins.FEBS open bio · 2026Article
- Deep learning-assisted tools to understand the structural biology of the synapse.Biomedical engineering letters · 2025Review
- Phosphoprofile reorganization of the actin binding protein Drebrin during long term depression.Frontiers in molecular neuroscience · 2025Article
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5 authors.
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Abstract
Drebrin (developmentally regulated brain protein) is a vital component of the Postsynaptic Density (PSD). It performs important biological roles as it interacts with the postsynaptic protein Homer and anchors the complete protein network to the cellular skeleton through actin filaments. Drebrin contains unique structural elements including an evolutionarily unconventional actin-depolymerizing factor homology (ADFH) domain that has lost its strong actin-binding ability, and a Single Alpha-Helix (SAH) motif harbored by long flexible regions. In vivo studies have suggested that a disordered segment in Drebrin plays a key role in binding filamentous actin, yet the atomic-level characterization of the binding interface between these proteins has not been reported. To bridge this gap, we designed the intrinsically disordered construct D233 and employed 3D (HN)CO(CO)NH NMR spectroscopy to accomplish a near-complete backbone resonance assignment. This work serves as an essential step toward a detailed structural and functional investigation of the interaction between Drebrin and F-Actin.
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