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Structural characterization of the N‐terminal part of the MERS‐CoV nucleocapsid by X‐ray diffraction and small‐angle X‐ray scattering
Author(s) -
Papageorgiou Nicolas,
Lichière Julie,
Baklouti Amal,
Ferron François,
Sévajol Marion,
Canard Bruno,
Coutard Bruno
Publication year - 2016
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798315024328
Subject(s) - small angle x ray scattering , terminal (telecommunication) , diffraction , crystallography , x ray , domain (mathematical analysis) , monomer , x ray crystallography , scattering , amino terminal , resolution (logic) , physics , materials science , chemistry , optics , peptide sequence , computer science , gene , biochemistry , nuclear magnetic resonance , mathematics , telecommunications , mathematical analysis , artificial intelligence , polymer
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.