The 1H, 15N and 13C resonance assignments of dengue virus capsid protein with the deletion of the intrinsically disordered N-terminal region

被引:0
作者
Barbosa, Glauce M. [1 ]
Morando, Maria A. [1 ,2 ]
Da Poian, Andrea T. [1 ]
Almeida, Fabio C. L. [1 ,3 ]
机构
[1] Fed Univ Rio De Janeiro UFRJ, Inst Med Biochem Leopoldo Meis IBqM, Rio De Janeiro, RJ, Brazil
[2] Fiocruz MS, Ctr Desenvolvimento Tecnol Saude, BR-21040361 Rio De Janeiro, Brazil
[3] Univ Fed Rio de Janeiro, Natl Ctr Struct Biol & Bioimaging CENABIO, Rio De Janeiro, RJ, Brazil
关键词
Dengue Virus; Capsid Protein; NMR; Capsid assembly; Intrinsically disordered region;
D O I
10.1007/s12104-022-10115-1
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Dengue virus belongs to the Flaviviridae family, being responsible for an endemic arboviral disease in humans. It is an enveloped virus, whose genome is a positive-stranded RNA packaged by the capsid protein. Dengue virus capsid protein (DENVC) forms homodimers in solution organized in 4 alpha-helices and an intrinsically disordered N-terminal region. The N-terminal region is involved in the binding of membranous structures in host cells and in the recognition of nucleotides. Here we report the H-1, N-15 and C-13 resonance assignments of the DENVC with the deletion of the first 19 intrinsically disordered residues. The backbone chemical shift perturbations suggest changes in the alpha 1 and alpha 2 helices between full length and the truncated proteins.
引用
收藏
页码:23 / 26
页数:4
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