Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/83047
Title: Secondary Structure and Membrane Topology of the Full-Length Dengue Virus NS4B in Micelles
Authors: Li, Yan
Wong, Ying Lei
Lee, Michelle Yueqi
Li, Qingxin
Wang, Qing-Yin
Lescar, Julien
Shi, Pei-Yong
Kang, CongBao
Keywords: Dengue-Virus
Membranproteine
Issue Date: 2016
Source: Li, Y., Wong, Y. L., Lee, M. Y., Li, Q., Wang, Q.-Y., Lescar, J., et al. (2016). Secondary Structure and Membrane Topology of the Full-Length Dengue Virus NS4B in Micelles. Angewandte Chemie International Edition, 55(39), 12068-12072.
Series/Report no.: Angewandte Chemie International Edition
Abstract: Dengue virus nonstructural protein 4B (NS4B) is a membrane protein consisting of 248 residues with a crucial role in virus replication and interference with the host innate immunity. The dengue virus serotype 3 NS4B was reconstituted into lyso-myristoyl phosphatidylglycerol (LMPG) micelles. Backbone resonance assignment of NS4B was obtained using conventional solution NMR experiments. Further studies suggested that NS4B contained eleven helices and six of them form five potential transmembrane regions. This study provides atomic level information for an important drug target to control flavivirus infections.
URI: https://hdl.handle.net/10356/83047
http://hdl.handle.net/10220/42374
ISSN: 1433-7851
DOI: 10.1002/anie.201606609
Rights: © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. This is the author created version of a work that has been peer reviewed and accepted for publication by Angewandte Chemie International Edition, WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1002/anie.201606609].
Fulltext Permission: open
Fulltext Availability: With Fulltext
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