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TitleStructural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering.
Journal, issue, pagesActa Crystallogr D Struct Biol, Vol. 72, Issue Pt 2, Page 192-202, Year 2016
Publish dateJan 22, 2016
AuthorsNicolas Papageorgiou / Julie Lichière / Amal Baklouti / François Ferron / Marion Sévajol / Bruno Canard / Bruno Coutard /
PubMed AbstractThe 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 ...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.
External linksActa Crystallogr D Struct Biol / PubMed:26894667 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution2.48 Å
Structure data

SASDBQ3:
Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164)
Method: SAXS/SANS

PDB-4ud1:
Structure of the N Terminal domain of the MERS CoV nucleocapsid
Method: X-RAY DIFFRACTION / Resolution: 2.48 Å

Chemicals

ChemComp-NH4:
AMMONIUM ION

ChemComp-IMD:
IMIDAZOLE

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • middle east respiratory syndrome coronavirus
KeywordsVIRAL PROTEIN / RNA BINDING DOMAIN

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