Abstract
The crystal structures of thymidine kinase from herpes simplex virus type-1 complexed with its natural substrate deoxythymidine (dT) and complexed with the guanosine analogue Ganciclovir have been solved. Both structures are in the C2221 crystal form with two molecules per asymmetric unit related by a non-crystal lographic two-fold axis. The present models have been refined to 2.8 Å and 2.2 Å, with crystal lographic R factors of 24.1% and 23.3% for the dT and Ganciclovir complexes respectively, without the inclusion of any solvent molecules. The core of the molecule exhibits high structural homology with adenylate kinase and other nucleotide binding proteins. These structural similarities provide an insight into the mechanism of nucleoside phosphorylation by thymidine kinase.
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Brown, D., Visse, R., Sandhu, G. et al. Crystal structures of the thymidine kinase from herpes simplex virus type-I in complex with deoxythymidine and Ganciclovir. Nat Struct Mol Biol 2, 876–881 (1995). https://doi.org/10.1038/nsb1095-876
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DOI: https://doi.org/10.1038/nsb1095-876
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