Biomolecular NMR Assignments

, Volume 12, Issue 1, pp 11–14 | Cite as

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

  • Nazimuddin Khan
  • David Ban
  • Pablo Trigo-Mourino
  • Marta G. Carneiro
  • Manfred Konrad
  • Donghan Lee
  • T. Michael Sabo


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.


Enzyme Guanylate kinase (GMPK) NMR assignment Nucleotide kinase 



We thank Prof. Dr. Christian Griesinger for providing measurement time and for valuable discussions related to the project. This research was supported by a DAAD scholarship (to NK), the Max Planck Society and by start-up funds provided by the James Graham Brown Foundation.


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Copyright information

© Springer Science+Business Media B.V. 2017

Authors and Affiliations

  1. 1.James Graham Brown Cancer Center, Department of MedicineUniversity of LouisvilleLouisvilleUSA
  2. 2.Enzyme Biochemistry GroupMax Planck Institute for Biophysical ChemistryGöttingenGermany
  3. 3.Department for NMR-Based Structural BiologyMax Planck Institute for Biophysical ChemistryGöttingenGermany
  4. 4.ZoBio B.V.LeidenThe Netherlands

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