Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants’ improved kinetics with the HIV prodrug metabolite AZTMP
- 17 November 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 304 (1) , 43-53
- https://doi.org/10.1006/jmbi.2000.4175
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Modifying Human Thymidylate Kinase to Potentiate Azidothymidine ActivationJournal of Biological Chemistry, 1999
- Structural basis for efficient phosphorylation of 3′-azidothymidine monophosphate by Escherichia coli thymidylate kinaseProceedings of the National Academy of Sciences, 1998
- Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation.Nature Structural & Molecular Biology, 1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constantsJournal of Applied Crystallography, 1993
- Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 Å resolutionJournal of Molecular Biology, 1992
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- Effects of 3′-azido-3′-deoxythymidine on the deoxynucleotide triphosphate pools of cultured human cellsBiochemical and Biophysical Research Communications, 1988
- Refined structure of porcine cytosolic adenylate kinase at 2.1 Å resolutionJournal of Molecular Biology, 1988
- Phosphorylation of 3'-azido-3'-deoxythymidine and selective interaction of the 5'-triphosphate with human immunodeficiency virus reverse transcriptase.Proceedings of the National Academy of Sciences, 1986