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

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

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_springer_journals_10_1038_nsb0897_601

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

About this item

Full title

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

Author / Creator

Lavie, Arnon , Vetter, Ingrid R. , Konrad, Manfred , Goody, Roger S. , Reinstein, Jochen and Schlichting, Ilme

Publisher

London: Nature Publishing Group UK

Journal title

Nature Structural Biology, 1997-08, Vol.4 (8), p.601-604

Language

English

Formats

Articles

Publication information

Publisher

London: Nature Publishing Group UK

Subjects

More information

Scope and Contents

Contents

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.

Alternative Titles

Full title

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

Authors, Artists and Contributors

Author / Creator

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_springer_journals_10_1038_nsb0897_601

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_springer_journals_10_1038_nsb0897_601

Other Identifiers

ISSN

1072-8368

E-ISSN

1545-9985

DOI

10.1038/nsb0897-601

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