The solution structure of the bovine leukaemia virus matrix protein and similarity with lentiviral matrix proteins.
In the mature virion, retroviral matrix proteins are found in association with the inner face of the viral membrane. They play a critical role in determining the morphogenesis of virus assembly. We have determined the three-dimensional solution structure of the bovine leukaemia virus (BLV) matrix protein by heteronuclear nuclear magnetic resonance. The protein contains four principal helices that are joined by short, partially structured loops. Despite no sequence similarity with the lentiviruses, the structure shows an intriguing homology with the equivalent protein from the human and simian immunodeficiency viruses. A root-mean-square deviation of 3.78 angstrom is observed over the backbone atoms of 36 equivalent helical positions. The similarity implies a possible common assembly unit for the matrix proteins of type C retroviruses.
Matthews
S
S
Department of Biochemistry, Imperial College of Science, Technology and Medicine, University of London, UK. sjm@bioch.ox.ac.uk
Mikhailov
M
M
Burny
A
A
Roy
P
P
D000595:Amino Acid Sequence; D015683:Gene Products, gag / Q000737:chemistry* / Q000235:genetics; D005982:Glutathione Transferase / Q000235:genetics; D016086:Lentivirus / Q000737:chemistry* / Q000235:genetics; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000235:genetics
D015683:Gene Products, gag; D011993:Recombinant Fusion Proteins; D014763:Viral Matrix Proteins; C080098:matrix-associated p15, bovine leukemia virus; D005982:Glutathione Transferase