Backbone 1H, 15N and 13C resonance assignments for dengue NS2B without the NS3 protease cofactor region in detergent micelles

IF 0.8 4区 生物学 Q4 BIOPHYSICS Biomolecular NMR Assignments Pub Date : 2023-07-05 DOI:10.1007/s12104-023-10142-6
Qingxin Li, Hui Qi Ng, Ying Ru Loh, CongBao Kang
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Abstract

Dengue virus is an important human pathogen affecting people especially in tropical and subtropical regions. Its genome encodes seven non-structural proteins that are important for viral assembly and replication. Dengue NS2B is a membrane protein containing four transmembrane helices and involved in protein-protein interactions. Its transmembrane helices are critical for location of NS2B on the cell membrane while one cytoplasmic region composed of approximately 40 amino acids serves as a cofactor of viral NS3 protease by forming a tight complex with the N-terminal region of NS3. Here, we report the backbone resonance assignments for a dengue NS2B construct referred to as mini-NS2B containing only the transmembrane regions without NS3 cofactor region in detergent micelles. Mini-NS2B exhibits well-dispersed cross-peaks in the 1H-15N-HSQC spectrum and contains four helices in solution. The available mini-NS2B and its assignment will be useful for determining the structure of NS2B and identifying small molecules binding to the transmembrane regions.

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洗涤剂胶束中不含NS3蛋白酶辅因子区的登革NS2B的主链1H、15N和13C共振分配
登革热病毒是一种重要的人类病原体,影响着热带和亚热带地区的人们。它的基因组编码七种对病毒组装和复制很重要的非结构蛋白。登革热NS2B是一种含有四个跨膜螺旋并参与蛋白质-蛋白质相互作用的膜蛋白。其跨膜螺旋对于NS2B在细胞膜上的定位至关重要,而由大约40个氨基酸组成的一个细胞质区域通过与NS3的N末端区域形成紧密复合物而充当病毒NS3蛋白酶的辅因子。在这里,我们报道了登革热NS2B构建体(称为mini-NS2B)的主链共振分配,该构建体在洗涤剂胶束中仅包含不含NS3辅因子区域的跨膜区域。Mini-NS2B在1H-15N-HSQC光谱中表现出良好分散的交叉峰,并且在溶液中含有四个螺旋。可用的mini-NS2B及其分配将有助于确定NS2B的结构和鉴定与跨膜区域结合的小分子。
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来源期刊
Biomolecular NMR Assignments
Biomolecular NMR Assignments 生物-光谱学
CiteScore
1.70
自引率
11.10%
发文量
59
审稿时长
6-12 weeks
期刊介绍: Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
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