Backbone ¹H, ¹³C and ¹⁵N resonance assignments of dengue virus NS2B-NS3p in complex with aprotinin

Biomol NMR Assign. 2013 Oct;7(2):137-9. doi: 10.1007/s12104-012-9395-9. Epub 2012 May 24.

Abstract

Dengue virus, belongs to Flaviviridae, is an arthropod transmitted virus that threatens millions of people's lives. As with other flaviviruses, a positive single-stranded 11-kilobases RNA in the dengue virus genome encodes three structural proteins (capsid protein C, membrane protein M, and envelope protein E) and seven non-structural proteins (NS1, NS2A, NS2B, NS3, NS4A, NS4B, and NS5). The two component protease NS2B-NS3p is essential for viral replication and is believed to be a potential antiviral drug target. Aprotinin, a native inhibitor, is proved to retard the activity of NS2B-NS3p. The backbone assignments of NS2B-NS3p will be essential for determining the high resolution solution structure of NS2B-NS3p and screening new antiviral drugs. Herein, we report the backbone (1)H, (15)N, (13)C resonance assignments of the N terminal fragment of NS2B (4.8 kDa) and NS3p (18.5 kDa) in complex with aprotinin (6.5 kDa) by high resolution NMR.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Aprotinin / chemistry*
  • Aprotinin / metabolism
  • Carbon Isotopes
  • Dengue Virus / metabolism*
  • Molecular Sequence Data
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protons
  • RNA Helicases / chemistry
  • RNA Helicases / metabolism
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / metabolism
  • Viral Nonstructural Proteins / chemistry*
  • Viral Nonstructural Proteins / metabolism*

Substances

  • Carbon Isotopes
  • NS3 protein, flavivirus
  • Nitrogen Isotopes
  • Protons
  • Viral Nonstructural Proteins
  • Aprotinin
  • Serine Endopeptidases
  • RNA Helicases