Sabine Krickl

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Thymidine kinase (TK), which is induced by Herpes Simplex Virus 1 (HSV1), plays a key role in the antiviral activity of guanine derivatives such as aciclovir (ACV). In contrast, ACV shows only low affinity to the corresponding host cell enzyme. In order to define the differences in substrate binding of the two enzymes on molecular level, models for the(More)
Adjacent peptide segments covering the complete sequence of herpes-simplex-virus type-1 thymidine kinase (HSV1-TK) of 376 amino acids were synthesized in order to experimentally verify the three-dimensional structure of the HSV1-TK active site, which was previously determined by molecular modeling. 26 peptides have been prepared by multiple solid-phase(More)
The amino acid sequence of 14 thymidine kinases and three other nucleotide binding enzymes have been compared by alignment of their primary and secondary structure. The overall alignment revealed five homologous regions, which are supposed to be part of the active site with a common three dimensional structure. Analysis of mutant enzymes brings further(More)
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