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

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, 601-604. doi:10.1038/nsb0897-601.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002A-CD2E-B Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002A-CDC7-F
Genre: Journal Article

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Lavie, A., Author
Vetter, I. R., Author
Konrad, M.1, Author           
Goody, R. S., Author
Reinstein, J., Author
Schlichting, I., Author
Affiliations:
1Research Group of Enzyme Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578612              

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 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.

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Language(s): eng - English
 Dates: 1997
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/nsb0897-601
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Title: Nature Structural Biology
Source Genre: Journal
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Pages: - Volume / Issue: 4 Sequence Number: - Start / End Page: 601 - 604 Identifier: -