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(1)H, (13)C and (15)N resonance assignment of backbone and IVL-methyl side chain of the S135A mutant NS3pro/NS2B protein of Dengue II virus reveals unique secondary structure features in solution

The serotype II Dengue (DENV 2) virus is the most prevalent of all four known serotypes. Herein, we present nearly complete (1)H, (15)N, and (13)C backbone and (1)H, (13)C isoleucine, valine, and leucine methyl resonance assignment of the apo S135A catalytically inactive variant of the DENV 2 protea...

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Autores principales: Agback, Peter, Lesovoy, Dmitry M., Han, Xiao, Sun, Renhua, Sandalova, Tatyana, Agback, Tatiana, Achour, Adnane, Orekhov, Vladislav Yu.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9068680/
https://www.ncbi.nlm.nih.gov/pubmed/35149939
http://dx.doi.org/10.1007/s12104-022-10071-w
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author Agback, Peter
Lesovoy, Dmitry M.
Han, Xiao
Sun, Renhua
Sandalova, Tatyana
Agback, Tatiana
Achour, Adnane
Orekhov, Vladislav Yu.
author_facet Agback, Peter
Lesovoy, Dmitry M.
Han, Xiao
Sun, Renhua
Sandalova, Tatyana
Agback, Tatiana
Achour, Adnane
Orekhov, Vladislav Yu.
author_sort Agback, Peter
collection PubMed
description The serotype II Dengue (DENV 2) virus is the most prevalent of all four known serotypes. Herein, we present nearly complete (1)H, (15)N, and (13)C backbone and (1)H, (13)C isoleucine, valine, and leucine methyl resonance assignment of the apo S135A catalytically inactive variant of the DENV 2 protease enzyme folded as a tandem formed between the serine protease domain NS3pro and the cofactor NS2B, as well as the secondary structure prediction of this complex based on the assigned chemical shifts using the TALOS-N software. Our results provide a solid ground for future elucidation of the structure and dynamic of the apo NS3pro/NS2B complex, key for adequate development of inhibitors, and a thorough molecular understanding of their function(s). SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s12104-022-10071-w.
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spelling pubmed-90686802022-05-07 (1)H, (13)C and (15)N resonance assignment of backbone and IVL-methyl side chain of the S135A mutant NS3pro/NS2B protein of Dengue II virus reveals unique secondary structure features in solution Agback, Peter Lesovoy, Dmitry M. Han, Xiao Sun, Renhua Sandalova, Tatyana Agback, Tatiana Achour, Adnane Orekhov, Vladislav Yu. Biomol NMR Assign Article The serotype II Dengue (DENV 2) virus is the most prevalent of all four known serotypes. Herein, we present nearly complete (1)H, (15)N, and (13)C backbone and (1)H, (13)C isoleucine, valine, and leucine methyl resonance assignment of the apo S135A catalytically inactive variant of the DENV 2 protease enzyme folded as a tandem formed between the serine protease domain NS3pro and the cofactor NS2B, as well as the secondary structure prediction of this complex based on the assigned chemical shifts using the TALOS-N software. Our results provide a solid ground for future elucidation of the structure and dynamic of the apo NS3pro/NS2B complex, key for adequate development of inhibitors, and a thorough molecular understanding of their function(s). SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s12104-022-10071-w. Springer Netherlands 2022-02-12 2022 /pmc/articles/PMC9068680/ /pubmed/35149939 http://dx.doi.org/10.1007/s12104-022-10071-w Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Agback, Peter
Lesovoy, Dmitry M.
Han, Xiao
Sun, Renhua
Sandalova, Tatyana
Agback, Tatiana
Achour, Adnane
Orekhov, Vladislav Yu.
(1)H, (13)C and (15)N resonance assignment of backbone and IVL-methyl side chain of the S135A mutant NS3pro/NS2B protein of Dengue II virus reveals unique secondary structure features in solution
title (1)H, (13)C and (15)N resonance assignment of backbone and IVL-methyl side chain of the S135A mutant NS3pro/NS2B protein of Dengue II virus reveals unique secondary structure features in solution
title_full (1)H, (13)C and (15)N resonance assignment of backbone and IVL-methyl side chain of the S135A mutant NS3pro/NS2B protein of Dengue II virus reveals unique secondary structure features in solution
title_fullStr (1)H, (13)C and (15)N resonance assignment of backbone and IVL-methyl side chain of the S135A mutant NS3pro/NS2B protein of Dengue II virus reveals unique secondary structure features in solution
title_full_unstemmed (1)H, (13)C and (15)N resonance assignment of backbone and IVL-methyl side chain of the S135A mutant NS3pro/NS2B protein of Dengue II virus reveals unique secondary structure features in solution
title_short (1)H, (13)C and (15)N resonance assignment of backbone and IVL-methyl side chain of the S135A mutant NS3pro/NS2B protein of Dengue II virus reveals unique secondary structure features in solution
title_sort (1)h, (13)c and (15)n resonance assignment of backbone and ivl-methyl side chain of the s135a mutant ns3pro/ns2b protein of dengue ii virus reveals unique secondary structure features in solution
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9068680/
https://www.ncbi.nlm.nih.gov/pubmed/35149939
http://dx.doi.org/10.1007/s12104-022-10071-w
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