Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus

J Mol Biol. 1998 Jun 19;279(4):921-8. doi: 10.1006/jmbi.1998.1788.


A biologically active construct of the retroviral M domain from the avian Rous sarcoma virus is defined and its solution structure described. This M domain is fully active in budding and infectivity without myristylation. In spite of a sequence homology level that suggests no relationship among M domains and the family of matrix proteins in mammalian retroviruses, the conserved structural elements of a central core allow an M domain sequence motif to be described for all retroviruses. The surface of the M domain has a highly clustered positive patch comprised of sequentially distant residues. An analysis of the backbone dynamics, incorporating rotational anisotropy, is used to estimate the thermodynamics of proposed domain oligomerization.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Avian Sarcoma Viruses / chemistry*
  • Molecular Sequence Data
  • Protein Conformation
  • Retroviridae Proteins / chemistry*
  • Retroviridae Proteins / genetics
  • Sequence Alignment
  • Sequence Analysis
  • Structure-Activity Relationship
  • Viral Matrix Proteins / chemistry*
  • Viral Matrix Proteins / genetics


  • Retroviridae Proteins
  • Viral Matrix Proteins