4.2 Article

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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出版社

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2059798315024328

关键词

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

资金

  1. SILVER Large Scale Collaborative Project of the European Union Seventh Framework [260644]
  2. French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10-INSB-05-01]

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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 angstrom. 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.

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