1H, 13C and 15N resonance assignment of human guanylate kinase
| Autor: | David Ban, Manfred Konrad, Marta G. Carneiro, Nazimuddin Khan, Donghan Lee, T. Michael Sabo, Pablo Trigo-Mouriño |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification 030102 biochemistry & molecular biology Guanylate kinase Nucleoside analogue Chemistry Stereochemistry Substrate (chemistry) Resonance Biochemistry 03 medical and health sciences 030104 developmental biology Enzyme Structural Biology medicine Side chain Phosphorylation Nucleoside medicine.drug |
| Zdroj: | Biomolecular NMR Assignments. 12:11-14 |
| ISSN: | 1874-270X 1874-2718 |
| DOI: | 10.1007/s12104-017-9771-6 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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