Variation in Active Site Amino Residues of H1N1 Swine Flu Neuraminidase

摘要

In this paper, we report the variations of amino acid residues between H5N1 and H1N1 swine flu neuraminidase sequences at protein level. Random search in NCBI Flu database resulted in Canadian viral gene and analysis using blast technique revealed sites that are variant among sequences for which 3-dimensional structures were known. PDB summary database and multiple alignments were employed for validatin of the results. Based on the mutations observed within active site region, homology derived model was constructed using swiss-pdb viewer. The residue variation observed was with respect to Tyr347 in H5N1 versus Asn344 in H1N1 neuraminidase sequence, which re-sulted in geometrical modification of ligand binding domain.