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 |