Literature DB >> 26894667

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

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


The full text for this article, hosted at http://journals.iucr.org, is unavailable due to technical difficulties. Supporting information for this article can be found http://scripts.iucr.org/cgi-bin/paper?mn5105
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