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Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation.

作者信息

Lavie A, Vetter I R, Konrad M, Goody R S, Reinstein J, Schlichting I

出版信息

Nat Struct Biol. 1997 Aug;4(8):601-4. doi: 10.1038/nsb0897-601.

DOI:10.1038/nsb0897-601
PMID:9253404
Abstract
摘要

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Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation.
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AZT monophosphate knocks thymidylate kinase for a loop.
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Structural requirements for efficient phosphorylation of nucleotide analogs by human thymidylate kinase.人胸苷酸激酶对核苷酸类似物进行有效磷酸化的结构要求。
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Structural basis for the efficient phosphorylation of AZT-MP (3'-azido-3'-deoxythymidine monophosphate) and dGMP by Plasmodium falciparum type I thymidylate kinase.疟原虫 I 型胸苷酸激酶催化 AZT-MP（3'-叠氮-3'-脱氧胸苷一磷酸）和 dGMP 高效磷酸化的结构基础。
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Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP.增强齐多夫定（AZT）的激活作用：野生型和突变型人胸苷酸激酶的结构揭示了突变体与HIV前药代谢物AZTMP动力学改善的原因。
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The crystal structure of Mycobacterium tuberculosis thymidylate kinase in complex with 3'-azidodeoxythymidine monophosphate suggests a mechanism for competitive inhibition.结核分枝杆菌胸苷酸激酶与3'-叠氮脱氧胸苷单磷酸复合物的晶体结构揭示了一种竞争性抑制机制。
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Structural basis for efficient phosphorylation of 3'-azidothymidine monophosphate by Escherichia coli thymidylate kinase.大肠杆菌胸苷酸激酶高效磷酸化3'-叠氮胸苷单磷酸的结构基础。
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