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

TitleSolution structure and dynamics of the bioactive retroviral M domain from rous sarcoma virus
Publication TypeJournal Articles
Year of Publication1998
AuthorsMcDonnell JM, Fushman D, Cahill SM, Zhou W, Wolven A, Wilson CB, Nelle TD, Resh MD, Wills J, Cowburn D
JournalJournal of Molecular Biology
Volume279
Issue4
Pagination921 - 928
Date Published1998/06/19/
ISBN Number0022-2836
Keywordsheteronuclear NMR spectroscopy, protein dynamics, RSV matrix protein, sequence homology, three-dimensional structure
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.

URLhttp://www.sciencedirect.com/science/article/pii/S0022283698917880
DOI10.1006/jmbi.1998.1788