期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1848, 期 10, 页码 2244-2252出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2015.06.010
关键词
Membrane protein; NMR; NS2B; Dengue virus; Protein dynamics
资金
- A*STAR JCO grants [1331A028, 1231B015]
Non-structural (NS) proteins of dengue virus (DENV) are important for viral replication. There are four membrane proteins that are coded by viral genome. NS2B was shown to be one of the membrane proteins and its main function was confirmed to regulate viral protease activity. Its membrane topology is still not known because only few studies have been conducted to understand its structure. Here we report the determination of membrane topology of NS2B from DENV serotype 4 using NMR spectroscopy. NS2B of DENV4 was expressed and purified in detergent micelles. The secondary structure of NS2B was first defined based on backbone chemical resonance assignment. Four helices were identified in NS2B. The membrane topology of NS2B was defined based on relaxation analysis and paramagnetic relaxation enhancement experiments. The last three helices were shown to be more stable than the first helix. The NS3 protease cofactor region between alpha 2 and alpha 3 is highly dynamic. Our results will be useful for further structural and functional analysis of NS2B. (C) 2015 Elsevier B.V. All rights reserved.
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