期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 72, 期 -, 页码 192-202出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2059798315024328
关键词
MERS-CoV; nucleocapsid; structure; SAXS; RNA-binding domain
资金
- SILVER Large Scale Collaborative Project of the European Union Seventh Framework [260644]
- French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10-INSB-05-01]
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 angstrom. 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.
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