West Nile virus core protein; tetramer structure and ribbon formation.

Academic Article

Abstract

  • We have determined the crystal structure of the core (C) protein from the Kunjin subtype of West Nile virus (WNV), closely related to the NY99 strain of WNV, currently a major health threat in the U.S. WNV is a member of the Flaviviridae family of enveloped RNA viruses that contains many important human pathogens. The C protein is associated with the RNA genome and forms the internal core which is surrounded by the envelope in the virion. The C protein structure contains four alpha helices and forms dimers that are organized into tetramers. The tetramers form extended filamentous ribbons resembling the stacked alpha helices seen in HEAT protein structures.
  • Authors

    Published In

  • Structure  Journal
  • Keywords

  • Amino Acid Sequence, Crystallography, X-Ray, Molecular Sequence Data, Protein Structure, Quaternary, Protein Structure, Secondary, Viral Core Proteins, West Nile virus
  • Digital Object Identifier (doi)

    Author List

  • Dokland T; Walsh M; Mackenzie JM; Khromykh AA; Ee K-H; Wang S
  • Start Page

  • 1157
  • End Page

  • 1163
  • Volume

  • 12
  • Issue

  • 7