Self-assembly properties of a model RING domain Academic Article uri icon


MeSH Major

  • Viral Proteins


  • RING domains act in a variety of essential cellular processes but have no general function ascribed to them. Here, we observe that purified arenaviral protein Z, constituted almost entirely by its RING domain, self-assembles in vitro into spherical structures that resemble functional bodies formed by Z in infected cells. By using a variety of biophysical methods we provide a thermodynamic and kinetic framework for the RING-dependent self-assembly of Z. Assembly appears coupled to substantial conformational reorganization and changes in zinc coordination of site II of the RING. Thus, the rate-limiting nature of conformational reorganization observed in the folding of monomeric proteins can also apply to the assembly of macromolecular scaffolds. These studies describe a unique mechanism of nonfibrillar homogeneous self-assembly and suggest a general function of RINGs in the formation of macromolecular scaffolds that are positioned to integrate biochemical processes in cells.

publication date

  • January 22, 2002



  • Academic Article



  • eng

PubMed Central ID

  • PMC117363

Digital Object Identifier (DOI)

  • 10.1073/pnas.012317299

PubMed ID

  • 11792829

Additional Document Info

start page

  • 667

end page

  • 72


  • 99


  • 2