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

被引：85

作者：

Lavie, A

Vetter, IR

Konrad, M

Goody, RS

Reinstein, J

Schlichting, I

机构：

[1] MAX PLANCK INST MOL PHYSIOL,DEPT PHYS BIOCHEM,D-44139 DORTMUND,GERMANY

[2] MAX PLANCK INST MOL PHYSIOL,DEPT BIOL STRUCT,D-44139 DORTMUND,GERMANY

[3] MAX PLANCK INST BIOPHYS CHEM,DEPT MOL GENET,D-37018 GOTTINGEN,GERMANY

来源：

NATURE STRUCTURAL BIOLOGY | 1997年 / 4卷 / 08期

关键词：

D O I：

10.1038/nsb0897-601

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Structural comparison of thymidylate kinase complexed with either dTMP or with AZTMP suggests that the low phosphorylation rate of AZTMP is due to an induced P-loop movement.

引用

页码：601 / 604

页数：4

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