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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(8), 601-604. doi:10.1038/nsb0897-601.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-2395-B Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-2396-9
Genre: Journal Article
Alternative Title : Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation

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NatStructBiol_4_1997_601.pdf (Any fulltext), 627KB
 
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http://www.nature.com/nsmb/journal/v4/n8/pdf/nsb0897-601.pdf (Any fulltext)
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https://dx.doi.org/10.1038/nsb0897-601 (Any fulltext)
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 Creators:
Lavie, Amon, Author
Vetter, Ingrid R., Author
Konrad, Manfred, Author
Goody, Roger S.1, Author           
Reinstein, Jochen2, Author           
Schlichting, Ilme1, Author           
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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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: 1997-04-301997-06-251997-08-01
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 667257
DOI: 10.1038/nsb0897-601
URI: https://www.ncbi.nlm.nih.gov/pubmed/9253404
Other: 3261
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Title: Nature structural biology
Source Genre: Journal
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Publ. Info: New York, NY : Nature Pub. Co.
Pages: - Volume / Issue: 4 (8) Sequence Number: - Start / End Page: 601 - 604 Identifier: ISSN: 1072-8368
CoNE: https://pure.mpg.de/cone/journals/resource/111073404672000