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 language | English (US) |
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Pages (from-to) | 921-928 |
Number of pages | 8 |
Journal | Journal of Molecular Biology |
Volume | 279 |
Issue number | 4 |
DOIs | |
State | Published - Jun 19 1998 |
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology