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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/1455| Structure and oligomerization state of the C-terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein | |
| Nguyen, T Lichière, J Canard, B Papageorgiou, N Attoumani, S Ferron, F Coutard, B | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| Middle East respiratory syndrome coronavirus (MERS-CoV) is a human pathogen responsible for a severe respiratory illness that emerged in 2012. Structural information about the proteins that constitute the viral particle is scarce. In order to contribute to a better understanding of the nucleoprotein (N) in charge of RNA genome encapsidation, the structure of the C-terminal domain of N from MERS-CoV obtained using single-crystal X-ray diffraction is reported here at 1.97 Å resolution. The molecule is present as a dimer in the crystal structure and this oligomerization state is confirmed in solution, as measured by additional methods including small-angle X-ray scattering measurements. Comparisons with the structures of the C-terminal domains of N from other coronaviruses reveals a high degree of structural conservation despite low sequence conservation, and differences in electrostatic potential at the surface of the protein. | |
| Acta Crystallographica, Section D - Structural Biology | |
| 2019 | |
| Preimpreso | |
| https://coronavirus.1science.com/item/8b72ac8772cae7058e321d7797d7b25633b102b6 | |
| Inglés | |
| VIRUS RESPIRATORIOS | |
| Aparece en las colecciones: | Artículos científicos |
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