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- W2087211300 abstract "The amino acid sequences of the core proteins of the alphaviruses Sindbis virus and Semliki Forest virus have been analyzed. The complete primary structures of both proteins are presented. At a few points in the N-terminal sequence regions the nucleotide sequences of the mRNA coding for the proteins (Garoff et al., Proc. Nat. Acad, Sci. USA77, 6376–6380,1980; Rice and Strauss, Proc. Nat. Acad. Sci. USA78, 2062–2066, 1981) have been used to align peptides. The N-terminal part of the proteins is rich in basic amino acids and proline, whereas the C-terminal region of the molecules does not show a preponderance of a specific type of amino acid. The transition between the two regions occurs in the region around amino acid residue 110. Whereas extensive sequence homology exists in the C-terminal part of both molecules (113 out of 163 amino acid residues are present in identical sequences) the sequence homology present in the N-terminal part is less pronounced. The data indicate that the physicochemical properties rather than the exact amino acid sequence are conserved in the N-terminal parts of the proteins. Both proteins contain the amino acid sequence Gly-Asp-Ser-Gly characteristic of eukaryotic serine proteases in the C-terminal highly conserved region of the molecule. Possible functions of both parts of the alphavirus-specific core proteins in the assembly of the virus and in the synthesis of viral structural proteins are discussed." @default.
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- W2087211300 date "1981-08-01" @default.
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- W2087211300 title "Primary structures of the core proteins of the alphaviruses semliki forest virus and sindbis virus" @default.
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- W2087211300 doi "https://doi.org/10.1016/0042-6822(81)90156-2" @default.
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