Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein

Christoph Wiedemann,Kingsley Benjamin Obika,Sandra Liebscher,Jan Jirschitzka,Oliver Ohlenschläger,Frank Bordusa

Biomolecular NMR Assignments（2022）

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摘要

The dysbindin domain-containing protein 1 (DBNDD1) is a conserved protein among higher eukaryotes whose structure and function are poorly investigated so far. Here, we present the backbone and side chain nuclear magnetic resonance assignments for the human DBNDD1 protein. Our chemical-shift based secondary structure analysis reveals the human DBNDD1 as an intrinsically disordered protein.

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关键词

Dysbindin domain-containing protein 1 (DBNDD1),Dystrobrevin-binding protein,Intrinsically disordered protein (IDP),Solution state nuclear magnetic resonance,Solution NMR,Backbone and side chain nuclear magnetic resonance assignments,Chemical shifts

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