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Matrix proteins associated with the viral membrane are important in the formation of the viral particle and in virus maturation. The 1.0 A crystal structure of the ecotropic Gammaretrovirus Moloney murine leukemia virus (M-MuLV) matrix protein reveals the conserved topology of other retroviral matrix proteins, despite undetectable sequence similarity. The N terminus (normally myristylated) is exposed and adjacent to a basic surface patch, features likely to contribute to membrane binding. The four proteins in the asymmetric unit make varied contacts. The M-MuLV matrix structure is intermediate, between those of the lentiviruses and other retroviruses. The protein fold appears to be maintained, in part, by the conservation of side chain packing, which may provide a useful tool for searching for weak distant similarities in proteins.


Journal article



Publication Date





1627 - 1636


Amino Acid Sequence, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Moloney murine leukemia virus, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Sequence Homology, Amino Acid, Viral Matrix Proteins