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

被引:44
作者
McDonnell, JM
Fushman, D
Cahill, SM
Zhou, WJ
Wolven, A
Wilson, CB
Nelle, TD
Resh, MD
Wills, J
Cowburn, D
机构
[1] Rockefeller Univ, New York, NY 10021 USA
[2] Mem Sloan Kettering Canc Ctr, New York, NY 10021 USA
[3] Penn State Univ, Sch Med, Dept Microbiol & Immunol, Hershey, PA 17033 USA
基金
美国国家卫生研究院;
关键词
RSV matrix protein; heteronuclear NMR-spectroscopy; three-dimensional structure; sequence homology; protein dynamics;
D O I
10.1006/jmbi.1998.1788
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1998 Academic Press Limited.
引用
收藏
页码:921 / 928
页数:8
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