Structural highlights
Function[A0A0D3MU51_9BETC] Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.[PIRNR:PIRNR003888][SAAS:SAAS01043082] Publication Abstract from PubMedMiddle 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 A 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. Structure and oligomerization state of the C-terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein.,Nguyen THV, Lichiere J, Canard B, Papageorgiou N, Attoumani S, Ferron F, Coutard B Acta Crystallogr D Struct Biol. 2019 Jan 1;75(Pt 1):8-15. doi:, 10.1107/S2059798318014948. Epub 2019 Jan 4. PMID:30644840[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 15:19, 27 February 2019.