Figure 3

NS5A structure changes were studied by using mutations present in our samples. Two of the mutations 2309 (Ala to Ser) and 2326 (Gly to Ala) are present in the transcriptional activation domain. (A) Partial structure of NS5A with native residue Ala at position 331 (position 2309 of the poly-protein). (B) The first mutation at location 2309 (Ala to Ser) changes the backbone of the amino acid due to the presence of a OH group in the side chain of the new amino acid. The native residue (Ala) is non-polar and more hydrophobic than the mutant, which is a polar one. (C) Partial structure of NS5A with native residue Gly at position 348 (position 2326 of the poly-protein). (D) Mutation at location 2326 (Gly to Ala). The mutant residue is bigger than the native Glycine. The native residue is the most flexible residue and it is possible that this residue is needed at this position to make a special backbone conformation or to facilitate movement of the protein.