Thermodynamic and mechanistic analysis of the functional properties of dengue virus NS3 helicase

被引：1

作者：

Incicco, J. Jeremias ^{[1
,2
]}

Cababie, Leila A. ^{[1
,2
]}

Sarto, Carolina ^{[3
]}

Adler, Natalia S. ^{[4
]}

Amrein, Fernando ^{[1
,2
]}

Mikkelsen, Evelyn ^{[1
,2
]}

Arrar, Mehrnoosh ^{[5
]}

Kaufman, Sergio B. ^{[1
,2
]}

机构：

[1] Univ Buenos Aires, CONICET, Inst Quim & Fis Quim Biol IQUIFIB, Junin 956, RA-1113 Buenos Aires, DF, Argentina

[2] Univ Buenos Aires, Fac Farm & Bioquim, Dept Quim Biol, Junin 956, RA-1113 Buenos Aires, DF, Argentina

[3] Univ Buenos Aires, CONICET, Inst Quim Biol Fac Ciencias Exactas & Nat IQUIBIC, Intendente Guiraldes 2160, RA-1428 Buenos Aires, DF, Argentina

[4] Ctr Invest Bionanociencias CIBION, CONICET, Godoy Cruz 2390, RA-1425 Buenos Aires, DF, Argentina

[5] Univ Buenos Aires, CONICET, Inst Calculo, Intendente Guiraldes 2160, RA-1428 Buenos Aires, DF, Argentina

来源：

BIOPHYSICAL REVIEWS | 2023年 / 15卷 / 04期

关键词：

NS3; Helicase; Molecular motors; Dengue; HEPATITIS-C VIRUS; RNA HELICASE; NONCOOPERATIVE BINDING; CHIKUNGUNYA VIRUS; CRYSTAL-STRUCTURE; ATPASE ACTIVITY; LARGE LIGANDS; PROTEIN; ENZYME; OLIGONUCLEOTIDE;

D O I：

10.1007/s12551-023-01101-5

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The Dengue Virus (DENV) non-structural protein 3 (NS3) is a multi-functional protein critical in the viral life cycle. The DENV NS3 is comprised of a serine protease domain and a helicase domain. The helicase domain itself acts as a molecular motor, either translocating in a unidirectional manner along single-stranded RNA or unwinding double-stranded RNA, processes fueled by the hydrolysis of nucleoside triphosphates. In this brief review, we summarize our contributions and ongoing efforts to uncover the thermodynamic and mechanistic functional properties of the DENV NS3 as an NTPase and helicase.

引用

页码：591 / 600

页数：10

共 62 条

[1] Insights into the product release mechanism of dengue virus NS3 helicase [J].