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Acta Crystallogr D Struct Biol. 2016 Feb;72(Pt 2):192-202. doi: 10.1107/S2059798315024328. Epub 2016 Jan 22.

Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering.

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CNRS, AFMB UMR 7257, 13288 Marseille, France.


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.


MERS-CoV; RNA-binding domain; SAXS; nucleocapsid; structure

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