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

MPS-Authors
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Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Reinstein,  Jochen
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Lavie, A., Vetter, I. R., Konrad, M., Goody, R. S., Reinstein, J., & Schlichting, I. (1997). Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation. Nature structural biology, 4(8), 601-604. doi:10.1038/nsb0897-601.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-2395-B
Abstract
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.