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

James M. McDonnell, David Fushman, Sean M. Cahill, Wenjun Zhou, Amy Wolven, Carol B. Wilson, Timothy D. Nelle, Marilyn D. Resh, John Wills, David Cowburn

Research output: Contribution to journalArticle

43 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)921-928
Number of pages8
JournalJournal of Molecular Biology
Volume279
Issue number4
DOIs
StatePublished - Jun 19 1998
Externally publishedYes

Keywords

  • Heteronuclear NMR spectroscopy
  • Protein dynamics
  • RSV matrix protein
  • Sequence homology
  • Three-dimensional structure

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    McDonnell, J. M., Fushman, D., Cahill, S. M., Zhou, W., Wolven, A., Wilson, C. B., Nelle, T. D., Resh, M. D., Wills, J., & Cowburn, D. (1998). Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus. Journal of Molecular Biology, 279(4), 921-928. https://doi.org/10.1006/jmbi.1998.1788