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Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery

Tuberculosis is an infectious disease caused by Mycobacterium tuberculosis, which triggers severe pulmonary diseases. Recently, multidrug/extensively drug-resistant tuberculosis strains have emerged and continue to threaten global health. Because of the development of drug-resistant tuberculosis, th...

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Autores principales: Kim, Do-Hee, Kang, Sung-Min, Lee, Bong-Jin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6151718/
https://www.ncbi.nlm.nih.gov/pubmed/28858250
http://dx.doi.org/10.3390/molecules22091447
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author Kim, Do-Hee
Kang, Sung-Min
Lee, Bong-Jin
author_facet Kim, Do-Hee
Kang, Sung-Min
Lee, Bong-Jin
author_sort Kim, Do-Hee
collection PubMed
description Tuberculosis is an infectious disease caused by Mycobacterium tuberculosis, which triggers severe pulmonary diseases. Recently, multidrug/extensively drug-resistant tuberculosis strains have emerged and continue to threaten global health. Because of the development of drug-resistant tuberculosis, there is an urgent need for novel antibiotics to treat these drug-resistant bacteria. In light of the clinical importance of M. tuberculosis, 2067 structures of M. tuberculsosis proteins have been determined. Among them, 52 structures have been solved and studied using solution nuclear magnetic resonance (NMR). The functional details based on structural analysis of M. tuberculosis using NMR can provide essential biochemical data for the development of novel antibiotic drugs. In this review, we introduce diverse structural and biochemical studies on M. tuberculosis proteins determined using NMR spectroscopy.
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spelling pubmed-61517182018-11-13 Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery Kim, Do-Hee Kang, Sung-Min Lee, Bong-Jin Molecules Review Tuberculosis is an infectious disease caused by Mycobacterium tuberculosis, which triggers severe pulmonary diseases. Recently, multidrug/extensively drug-resistant tuberculosis strains have emerged and continue to threaten global health. Because of the development of drug-resistant tuberculosis, there is an urgent need for novel antibiotics to treat these drug-resistant bacteria. In light of the clinical importance of M. tuberculosis, 2067 structures of M. tuberculsosis proteins have been determined. Among them, 52 structures have been solved and studied using solution nuclear magnetic resonance (NMR). The functional details based on structural analysis of M. tuberculosis using NMR can provide essential biochemical data for the development of novel antibiotic drugs. In this review, we introduce diverse structural and biochemical studies on M. tuberculosis proteins determined using NMR spectroscopy. MDPI 2017-08-31 /pmc/articles/PMC6151718/ /pubmed/28858250 http://dx.doi.org/10.3390/molecules22091447 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Kim, Do-Hee
Kang, Sung-Min
Lee, Bong-Jin
Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery
title Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery
title_full Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery
title_fullStr Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery
title_full_unstemmed Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery
title_short Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery
title_sort solution nmr studies of mycobacterium tuberculosis proteins for antibiotic target discovery
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6151718/
https://www.ncbi.nlm.nih.gov/pubmed/28858250
http://dx.doi.org/10.3390/molecules22091447
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