Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus.
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.
McDonnell
J M
JM
The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Fushman
D
D
Cahill
S M
SM
Zhou
W
W
Wolven
A
A
Wilson
C B
CB
Nelle
T D
TD
Resh
M D
MD
Wills
J
J
Cowburn
D
D
D000595:Amino Acid Sequence; D001358:Avian Sarcoma Viruses / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012191:Retroviridae Proteins / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment; D017421:Sequence Analysis; D013329:Structure-Activity Relationship; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000235:genetics
D012191:Retroviridae Proteins; D014763:Viral Matrix Proteins