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X-Ray Analysis of Azido-Thymidine Diphosphate Binding to Nucleoside Diphosphate Kinase

X-Ray Analysis of Azido-Thymidine Diphosphate Binding to Nucleoside Diphosphate Kinase

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_16017713

X-Ray Analysis of Azido-Thymidine Diphosphate Binding to Nucleoside Diphosphate Kinase

About this item

Full title

X-Ray Analysis of Azido-Thymidine Diphosphate Binding to Nucleoside Diphosphate Kinase

Publisher

United States: National Academy of Sciences of the United States of America

Journal title

Proceedings of the National Academy of Sciences - PNAS, 1997-07, Vol.94 (14), p.7162-7165

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences of the United States of America

More information

Scope and Contents

Contents

To be effective as antiviral agent, AZT (3′-azido-3′-deoxythymidine) must be converted to a triphosphate derivative by cellular kinases. The conversion is inefficient and, to understand why AZT diphosphate is a poor substrate of nucleoside diphosphate (NDP) kinase, we determined a 2.3- angstrom x-ray structure of a complex with the N119A point muta...

Alternative Titles

Full title

X-Ray Analysis of Azido-Thymidine Diphosphate Binding to Nucleoside Diphosphate Kinase

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_16017713

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_16017713

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.94.14.7162

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