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Journal Article

1H, 13C and 15N resonance assignment of human guanylate kinase.

MPS-Authors
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Khan,  N.
Research Group of Enzyme Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Trigo-Mourino,  P.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Carneiro,  M. G.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Konrad,  M.
Research Group of Enzyme Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Lee,  D.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Sabo,  T. M.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Khan, N., Ban, D., Trigo-Mourino, P., Carneiro, M. G., Konrad, M., Lee, D., et al. (2018). 1H, 13C and 15N resonance assignment of human guanylate kinase. Biomolecular NMR Assignments, 12(1), 11-14. doi:10.1007/s12104-017-9771-6.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-E41D-B
Abstract
Human guanylate kinase (hGMPK) is a critical enzyme that, in addition to phosphorylating its physiological substrate (d)GMP, catalyzes the second phosphorylation step in the conversion of anti-viral and anti-cancer nucleoside analogs to their corresponding active nucleoside analog triphosphates. Until now, a high-resolution structure of hGMPK is unavailable and thus, we studied free hGMPK by NMR and assigned the chemical shift resonances of backbone and side chain 1H, 13C, and 15N nuclei as a first step towards the enzyme's structural and mechanistic analysis with atomic resolution.