期刊
SCIENCE
卷 326, 期 5957, 页码 1279-1283出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1177634
关键词
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资金
- Marie-Curie RTN fellowship [MRTN-CT-2006-035599]
- French Fondation pour la Recherche Medicale
- French Agence Nationale pour la Recherche
- Merck-Serono
- MRC [MC_U130115834] Funding Source: UKRI
The respiratory syncytial virus (RSV) is an important human pathogen, yet neither a vaccine nor effective therapies are available to treat infection. To help elucidate the replication mechanism of this RNA virus, we determined the three-dimensional (3D) crystal structure at 3.3 angstrom resolution of a decameric, annular ribonucleoprotein complex of the RSV nucleoprotein (N) bound to RNA. This complex mimics one turn of the viral helical nucleocapsid complex, which serves as template for viral RNA synthesis. The RNA wraps around the protein ring, with seven nucleotides contacting each N subunit, alternating rows of four and three stacked bases that are exposed and buried within a protein groove, respectively. Combined with electron microscopy data, this structure provides a detailed model for the RSV nucleocapsid, in which the bases are accessible for readout by the viral polymerase. Furthermore, the nucleoprotein structure highlights possible key sites for drug targeting.
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