作者: Ioannis Nikas , John McLauchlan , Andrew J. Davison , William R. Taylor , J. Barklie Clements
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摘要: Herpes simplex virus type 1 (HSV-1) encodes a ribonucleotide reductase which comprises two polypeptides with sizes of 136,000 (RR1) and 38,000 mol. wt. (RR2). We have determined the entire DNA sequence specifying HSV-1 RR1 identified adjacent open reading frames in varicella-zoster (VZV) homology to HSV RR2; predicted for VZV RR2 are 87,000 35,000 respectively. Amino acid comparisons from other organisms indicate that contains unique N-terminal domain is absent apart HSV-2 RR1. These amino sequences poorly conserved between contrast remainder protein shows greater than 90% homology. Polypeptide structural predictions suggest may be separated into regions, namely, beta-sheet structure followed by nonstructured area. Across RR2, also reveal blocks acids different reductases, these important enzyme activity. From on blocks, we proposed location substrate binding site within centered three glycine residues region adopt beta-sheet/turn/alpha-helical structure; this approximates ADP nucleotide folds. Finally, propose promoters Epstein-Barr (EBV) transcripts evolved separate evolutionary routes.