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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.

Acta Crystallogr D Struct Biol.. 2016-02; 
Papageorgiou N, Lichière J, Baklouti A, Ferron F, Sévajol M, Canard B, Coutard B.
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Gene Synthesis ... 2.1. Protein production, purification and characterization. The codon-optimized DNA encoding the N-terminal region (amino acids 1–164; NTD + ) of the MERS-CoV nucleocapsid (strain Betacoronavirus England 1, accession No. KC164505) was synthesized by GenScript. ... Get A Quote

摘要

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 coro... More

关键词

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