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• W2064223379 endingPage "5800" @default.
• W2064223379 startingPage "5792" @default.
• W2064223379 abstract "The low toxicity of acyclovir (ACV) is mainly due to the fact that human nucleoside kinases have undetectable phosphorylation rates with this acyclic guanine analogue. In contrast, herpes virus thymidine kinase (HSV1-TK) readily activates ACV. We wanted to understand why human deoxycytidine kinase (dCK), which is related to HSV1-TK and phosphorylates deoxyguanosine, does not accept acyclic guanine analogues as substrates. Therefore, we crystallized dCK in complex with ACV at the nucleoside phosphoryl acceptor site and UDP at the phosphoryl donor site. The structure reveals that while ACV does bind at the dCK active site, it does so adopting a nonproductive conformation. Despite binding ACV, the enzyme remains in the open, inactive state. In comparison to ACV binding to HSV1-TK, in dCK, the nucleoside base adopts a different orientation related by about a 60 degrees rotation. Our analysis suggests that dCK would phosphorylate acyclic guanine analogues if they can induce a similar rotation." @default.
• W2064223379 created "2016-06-24" @default.
• W2064223379 creator A5004462439 @default.
• W2064223379 creator A5042486255 @default.
• W2064223379 creator A5079129780 @default.
• W2064223379 date "2010-07-14" @default.
• W2064223379 modified "2023-09-27" @default.
• W2064223379 title "The Sugar Ring of the Nucleoside Is Required for Productive Substrate Positioning in the Active Site of Human Deoxycytidine Kinase (dCK): Implications for the Development of dCK-Activated Acyclic Guanine Analogues" @default.
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• W2064223379 doi "https://doi.org/10.1021/jm1005379" @default.
• W2064223379 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2936711" @default.
• W2064223379 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20684612" @default.
• W2064223379 hasPublicationYear "2010" @default.
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