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
Qingxin Li, Hui Qi Ng, Ying Ru Loh, CongBao Kang
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引用次数: 0

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.

Abstract Image

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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