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The solution structure of the bovine leukaemia virus matrix protein and similarity with lentiviral matrix proteins.
Author(s) -
Matthews S.,
Mikhailov M.,
Burny A.,
Roy P.
Publication year - 1996
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1996.tb00691.x
Subject(s) - biology , viral matrix protein , matrix (chemical analysis) , structural similarity , similarity (geometry) , virus , virology , computational biology , genetics , biochemistry , computer science , materials science , image (mathematics) , artificial intelligence , composite material
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.