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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-E41D-B Version Permalink: http://hdl.handle.net/21.11116/0000-0003-74B2-1
Genre: Journal Article

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2478856.pdf (Publisher version), 893KB
 
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 Creators:
Khan, N.1, Author              
Ban, D., Author
Trigo-Mourino, P.2, Author              
Carneiro, M. G.2, Author              
Konrad, M.1, Author              
Lee, D.2, Author              
Sabo, T. M.2, Author              
Affiliations:
1Research Group of Enzyme Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578612              
2Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_578567              

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Free keywords: Enzyme; Guanylate kinase (GMPK); NMR assignment; Nucleotide kinase
 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.

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Language(s): eng - English
 Dates: 2017-08-312018-04
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1007/s12104-017-9771-6
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Title: Biomolecular NMR Assignments
Source Genre: Journal
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Pages: - Volume / Issue: 12 (1) Sequence Number: - Start / End Page: 11 - 14 Identifier: -