Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering.
Identifieur interne : 000E92 ( PubMed/Checkpoint ); précédent : 000E91; suivant : 000E93Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering.
Auteurs : Nicolas Papageorgiou [France] ; Julie Lichière [France] ; Amal Baklouti [France] ; François Ferron [France] ; Marion Sévajol [France] ; Bruno Canard [France] ; Bruno Coutard [France]Source :
- Acta crystallographica. Section D, Structural biology [ 2059-7983 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemistry : Middle East Respiratory Syndrome Coronavirus.
- Crystallization, Crystallography, X-Ray, Models, Molecular, Protein Multimerization, Protein Structure, Tertiary, Scattering, Small Angle.
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.
DOI: 10.1107/S2059798315024328
PubMed: 26894667
Affiliations:
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pubmed:26894667Le document en format XML
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<front><div type="abstract" xml:lang="en">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. </div>
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