The atomic structure of the bluetongue virus core

Nature. 1998 Oct 1;395(6701):470-8. doi: 10.1038/26694.


The structure of the core particle of bluetongue virus has been determined by X-ray crystallography at a resolution approaching 3.5 A. This transcriptionally active compartment, 700 A in diameter, represents the largest molecular structure determined in such detail. The atomic structure indicates how approximately 1,000 protein components self-assemble, using both the classical mechanism of quasi-equivalent contacts, which are achieved through triangulation, and a different method, which we term geometrical quasi-equivalence.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bluetongue virus / chemistry*
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • RNA, Viral / chemistry
  • Viral Core Proteins / chemistry*
  • Viral Core Proteins / metabolism


  • RNA, Viral
  • VP3 protein, Bluetongue virus
  • Viral Core Proteins
  • VP7 protein, orbivirus

Associated data

  • PDB/2BTV