Structural and kinetic evidence points to an induced loop movement in thymidylate kinase as leading to the limiting step in AZT activation in HIV therapy.
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References
Ma, Q., Bathurst, I.C., Barr, P.I. & Kenyon, G.L. Biochemistry 31, 1375–1379 (1992).
Balzarini, J., Herdewijn, P. & De, C.E. J. Biol. Chem. 264, 6127–6133 (1989).
Lavie, A., Vetta, I.R., Konrad, M., Goody, R.S., Reinstein, J. & Schlichting, I. Nature Struct. Biol. 4, 601–604 (1997).
Lavie, A., Schlichting, I., Vetta, I.R., Konrad, M., Reinstein, J. & Goody, R.S. Nature Med. 3, 922–924 (1997).
Yan, J.P. et al. J. Biol. Chem. 270, 22836–22841 (1995).
Tantillo, C. et al. J. Mol. Biol. 243, 369–387 (1994).
Ringe, D. Phil. Trans. Roy. Soc. London A 340, 273–284 (1992).
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Kenyon, G. AZT monophosphate knocks thymidylate kinase for a loop. Nat Struct Mol Biol 4, 595–597 (1997). https://doi.org/10.1038/nsb0897-595
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DOI: https://doi.org/10.1038/nsb0897-595
