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

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BIOMOLECULAR NMR ASSIGNMENTS
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SPRINGER
DOI: 10.1007/s12104-023-10142-6

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Dengue virus; NS2B; Membrane protein; Protein structure; Dynamics

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Dengue virus is a significant human pathogen in tropical and subtropical regions, and its genome encodes important non-structural proteins for assembly and replication. Dengue NS2B, a membrane protein involved in protein-protein interactions, has critical transmembrane helices and a cytoplasmic region that acts as a cofactor for viral NS3 protease. We have reported the backbone resonance assignments for a dengue NS2B construct called mini-NS2B, containing only transmembrane regions, which will aid in determining NS2B structure and identifying small molecules that bind to the transmembrane regions.
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 H-1-N-15-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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