Nuclear Magnetic Resonance Structure of the N-Terminal Domain of Nonstructural Protein 3 from the Severe Acute Respiratory Syndrome Coronavirus uri icon

abstract

  • This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. In addition to the four beta-strands and two alpha-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a feature that has not previously been observed in these proteins. Nuclear magnetic resonance chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA. Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence.

published proceedings

  • Journal of Virology

altmetric score

  • 3

author list (cited authors)

  • Serrano, P., Johnson, M. A., Almeida, M. S., Horst, R., Herrmann, T., Joseph, J. S., ... Wthrich, K.

citation count

  • 64

complete list of authors

  • Serrano, Pedro||Johnson, Margaret A||Almeida, Marcius S||Horst, Reto||Herrmann, Torsten||Joseph, Jeremiah S||Neuman, Benjamin W||Subramanian, Vanitha||Saikatendu, Kumar S||Buchmeier, Michael J||Stevens, Raymond C||Kuhn, Peter||Wüthrich, Kurt

publication date

  • August 2007