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-Structure paper
タイトル | 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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ジャーナル・号・ページ | Acta Crystallogr D Struct Biol, Vol. 72, Issue Pt 2, Page 192-202, Year 2016 |
掲載日 | 2016年1月22日 |
著者 | Nicolas Papageorgiou / Julie Lichière / Amal Baklouti / François Ferron / Marion Sévajol / Bruno Canard / Bruno Coutard / |
PubMed 要旨 | 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. |
リンク | Acta Crystallogr D Struct Biol / PubMed:26894667 / PubMed Central |
手法 | SAS (X-ray synchrotron) / X線回折 |
解像度 | 2.48 Å |
構造データ | SASDBQ3: PDB-4ud1: |
化合物 | ChemComp-NH4: ChemComp-IMD: ChemComp-GOL: ChemComp-HOH: |
由来 |
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キーワード | VIRAL PROTEIN / RNA BINDING DOMAIN |