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


Authors: 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.
Article Title: Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus
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.
Keywords: controlled study; sequence analysis; nonhuman; protein conformation; protein domain; mammalia; molecular dynamics; structure-activity relationship; aves; amino acid sequence; molecular sequence data; sequence alignment; rna viruses; thermodynamics; protein structure; sequence homology; viral matrix proteins; oligomerization; anisotropy; virus protein; myristylation; protein dynamics; rice stripe virus; three-dimensional structure; rous sarcoma oncovirus; rous sarcoma virus; avian sarcoma viruses; priority journal; article; retroviridae proteins; oncovirinae; heteronuclear nmr spectroscopy; rsv matrix protein
Journal Title: Journal of Molecular Biology
Volume: 279
Issue: 4
ISSN: 0022-2836
Publisher: Academic Press Inc., Elsevier Science  
Date Published: 1998-06-19
Start Page: 921
End Page: 928
Language: English
DOI: 10.1006/jmbi.1998.1788
PUBMED: 9642071
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 12 December 2016 -- Source: Scopus
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  1. Marilyn D Resh
    120 Resh