Resonance assignment of the intrinsically disordered actin-binding region of Drebrin

Varga Soma; Kaasen Julie Maibøll; Gáspári Zoltán; Péterfia Bálint; Mulder Frans A. A.: Resonance assignment of the intrinsically disordered actin-binding region of Drebrin.
BIOMOLECULAR NMR ASSIGNMENTS, -. pp. 1-5. ISSN 1874-2718 (2025)

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Folyóiratcikk

Szerző azonosítók:

Név	ORCID	MTMT szerző azonosító
Varga Soma		10079631
Kaasen Julie Maibøll
Gáspári Zoltán		10001271
Péterfia Bálint		10026672
Mulder Frans A. A.	0000-0001-9427-8406

Absztrakt (kivonat):

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.

Folyóirat címe:

BIOMOLECULAR NMR ASSIGNMENTS

Megjelenés éve:

2025

Kötet:

Oldalak:

pp. 1-5

ISSN:

1874-2718

Intézmény:

Pázmány Péter Katolikus Egyetem

Kar: