The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes

• Main Authors: Ferron F., Li Z., Danek E.I., Luo D., Wong Y., Coutard B., Lantez V., Charrel R., Canard B., Walz T., Lescar J.
• Other Authors: DUKE-NUS MEDICAL SCHOOL
• Format: Article
• Published: Public Library of Science 2020
• Subjects: guanine nucleotide binding protein; nucleoprotein; oligomer; ribonucleoprotein; RNA; complementary DNA; hybrid protein; nucleocapsid protein; virus RNA; amino terminal sequence; article; binding site; Bunyavirus; crystal structure; crystallization; crystallography; electron microscopy; hydrophobicity; in vivo study; molecular interaction; mutagenesis; nonhuman; nucleotide sequence; protein assembly; protein conformation; protein multimerization; Rift Valley fever bunyavirus; RNA binding; amino acid sequence; animal; chemical structure; chemistry; genetics; human; isolation and purification; metabolism; methodology; physiology; protein domain; sequence alignment; site directed mutagenesis; surface plasmon resonance; ultrastructure; virus assembly; X ray crystallography; Bunyaviridae; Phlebovirus; Rift Valley fever virus; Amino Acid Sequence; Animals; Crystallography, X-Ray; DNA, Complementary; Humans; Microscopy, Electron; Models, Molecular; Mutagenesis, Site-Directed; Nucleocapsid Proteins; Protein Interaction Domains and Motifs; Protein Multimerization; Recombinant Fusion Proteins; Ribonucleoproteins; RNA, Viral; Sequence Alignment; Surface Plasmon Resonance; Virus Assembly
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/165414
• Institution: National University of Singapore

10.1371/journal.ppat.1002030