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

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


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.

Keywords: MERS-CoV; RNA-binding domain; SAXS; nucleocapsid; structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Middle East Respiratory Syndrome Coronavirus / chemistry
  • Models, Molecular
  • Nucleocapsid Proteins / chemistry*
  • Protein Multimerization
  • Protein Structure, Tertiary
  • Scattering, Small Angle


  • Nucleocapsid Proteins