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

被引：3

作者：

Khan, Nazimuddin ^{[1
,2
]}

Ban, David ^{[1
]}

Trigo-Mourino, Pablo ^{[3
]}

Carneiro, Marta G. ^{[3
,4
]}

Konrad, Manfred ^{[2
]}

Lee, Donghan ^{[1
,3
]}

Sabo, T. Michael ^{[1
,3
]}

机构：

[1] Univ Louisville, Dept Med, James Graham Brown Canc Ctr, 505 S Hancock St, Louisville, KY 40202 USA

[2] Max Planck Inst Biophys Chem, Enzyme Biochem Grp, Fassberg 11, D-37077 Gottingen, Germany

[3] Max Planck Inst Biophys Chem, Dept NMR Based Struct Biol, Fassberg 11, D-37077 Gottingen, Germany

[4] ZoBio BV, Biopartner Bldg 2,JH Oortweg 19, NL-2333 CH Leiden, Netherlands

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2018年 / 12卷 / 01期

关键词：

Enzyme; Guanylate kinase (GMPK); NMR assignment; Nucleotide kinase; ESCHERICHIA-COLI; GMP KINASE; RECOMBINANT PROTEINS; NMR; MONOPHOSPHATE; SPECTROSCOPY; SPECTRA; EXPRESSION; COHERENCE; EFFICIENT;

D O I：

10.1007/s12104-017-9771-6

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

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 H-1, C-13, and N-15 nuclei as a first step towards the enzyme's structural and mechanistic analysis with atomic resolution.

引用

页码：11 / 14

页数：4

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