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重组单纯疱疹病毒1型胸苷激酶与胸苷和阿昔洛韦的相互作用:一项动力学研究。

Interaction of the recombinant herpes simplex virus type 1 thymidine kinase with thymidine and aciclovir: a kinetic study.

作者信息

Kussmann-Gerber S, Wurth C, Scapozza L, Pilger B D, Pliska V, Folkers G

机构信息

Department of Pharmacy, Swiss Federal Institute of Technology (ETH), Zürich, Switzerland.

出版信息

Nucleosides Nucleotides. 1999 Mar;18(3):311-30. doi: 10.1080/15257779908043078.

DOI:10.1080/15257779908043078
PMID:10358938
Abstract

Herpes Simplex Virus type 1 thymidine kinase (HSV 1 TK) is a key target for antiviral therapy and it phosphorylates a broad spectrum of nucleosides and nucleotides. We report the results from kinetic and inhibition experiments with HSV 1 TK, and show that there is a preferred, but not exclusive, binding order of substrates, i.e. dT binds prior to ATP. Furthermore, the results provide new informations on the mechanism of binding suggesting that HSV1 TK undergoes conformational changes during the catalytic cycle.

摘要

单纯疱疹病毒1型胸苷激酶(HSV 1 TK)是抗病毒治疗的关键靶点,它能磷酸化多种核苷和核苷酸。我们报告了HSV 1 TK的动力学和抑制实验结果,表明底物存在优先但非排他的结合顺序,即dT在ATP之前结合。此外,这些结果提供了关于结合机制的新信息,表明HSV1 TK在催化循环中会发生构象变化。

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Interaction of the recombinant herpes simplex virus type 1 thymidine kinase with thymidine and aciclovir: a kinetic study.重组单纯疱疹病毒1型胸苷激酶与胸苷和阿昔洛韦的相互作用:一项动力学研究。
Nucleosides Nucleotides. 1999 Mar;18(3):311-30. doi: 10.1080/15257779908043078.
2
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引用本文的文献

1
The effect of substrate binding on the conformation and structural stability of Herpes simplex virus type 1 thymidine kinase.底物结合对1型单纯疱疹病毒胸苷激酶构象和结构稳定性的影响。
Protein Sci. 2001 Jan;10(1):63-73. doi: 10.1110/ps.27401.