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| Title | Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering. |
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| Journal, issue, pages | Acta Crystallogr D Struct Biol, Vol. 72, Issue Pt 2, Page 192-202, Year 2016 |
| Publish date | Jan 22, 2016 |
Authors | Nicolas Papageorgiou / Julie Lichière / Amal Baklouti / François Ferron / Marion Sévajol / Bruno Canard / Bruno Coutard / ![]() |
| PubMed 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 ...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 links | Acta Crystallogr D Struct Biol / PubMed:26894667 / PubMed Central |
| Methods | SAS (X-ray synchrotron) / X-ray diffraction |
| Resolution | 2.48 Å |
| Structure data | ![]() SASDBQ3: ![]() PDB-4ud1: |
| Chemicals | ![]() ChemComp-NH4: ![]() ChemComp-IMD: ![]() ChemComp-GOL: ![]() ChemComp-HOH: |
| Source |
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Keywords | VIRAL PROTEIN / RNA BINDING DOMAIN |
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