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

doi:10.1007/s12104-022-10086-3

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

Biomol NMR Assign. 2022 Oct;16(2):237-246. doi: 10.1007/s12104-022-10086-3. Epub 2022 Apr 26.

Authors

Christoph Wiedemann^{1

2}, Kingsley Benjamin Obika³, Sandra Liebscher³, Jan Jirschitzka⁴, Oliver Ohlenschläger⁵, Frank Bordusa³

Affiliations

¹ Charles Tanford Protein Centre, Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Germany. christoph.wiedemann@uni-jena.de.
² Faculty of Chemistry and Earth Sciences, Institute of Organic Chemistry and Macromolecular Chemistry, Biostructural Interactions, Friedrich Schiller University Jena, Humboldtstraße 10, 07743, Jena, Germany. christoph.wiedemann@uni-jena.de.
³ Charles Tanford Protein Centre, Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Germany.
⁴ Department of Chemistry, Institute of Biochemistry, University of Cologne, Zülpicher Str. 47, 50674, Cologne, Germany.
⁵ Leibniz Institute on Aging - Fritz Lipmann Institute, Beutenbergstr. 11, 07745, Jena, Germany.

Abstract

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.

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

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Dysbindin
Humans
Intrinsically Disordered Proteins* / chemistry
Magnetic Resonance Spectroscopy
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary

Substances

Dysbindin
Intrinsically Disordered Proteins