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

被引：0
作者：
Nazimuddin Khan
David Ban
Pablo Trigo-Mourino
Marta G. Carneiro
Manfred Konrad
Donghan Lee
T. Michael Sabo
机构：
[1] University of Louisville,James Graham Brown Cancer Center, Department of Medicine
[2] Max Planck Institute for Biophysical Chemistry,Enzyme Biochemistry Group
[3] Max Planck Institute for Biophysical Chemistry,Department for NMR
[4] ZoBio B.V.,Based Structural Biology
来源：
Biomolecular NMR Assignments | 2018年 / 12卷
关键词：
Enzyme; Guanylate kinase (GMPK); NMR assignment; Nucleotide kinase;
D O I：
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学科分类号：
摘要：
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.
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页码：11 / 14
页数：3
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