| Literature DB >> 26894667 |
Nicolas Papageorgiou1, Julie Lichière1, Amal Baklouti1, François Ferron1, Marion Sévajol1, Bruno Canard1, Bruno Coutard1.
Abstract
The N protein of coronaviruses is a multifunctional protein that is organized into several domains. The N-terminal part is composed of an intrinsically disordered region (IDR) followed by a structured domain called the N-terminal domain (NTD). In this study, the structure determination of the N-terminal region of the MERS-CoV N protein via X-ray diffraction measurements is reported at a resolution of 2.4 Å. Since the first 30 amino acids were not resolved by X-ray diffraction, the structural study was completed by a SAXS experiment to propose a structural model including the IDR. This model presents the N-terminal region of the MERS-CoV as a monomer that displays structural features in common with other coronavirus NTDs.Entities:
Keywords: MERS-CoV; RNA-binding domain; SAXS; nucleocapsid; structure
Mesh:
Substances:
Year: 2016 PMID: 26894667 PMCID: PMC7159594 DOI: 10.1107/S2059798315024328
Source DB: PubMed Journal: Acta Crystallogr D Struct Biol ISSN: 2059-7983 Impact factor: 7.652