共 39 条
The role of surface basic amino acids of dengue virus NS3 helicase in viral RNA replication and enzyme activities
被引:13
作者:

Chiang, Pao-Yin
论文数: 0 引用数: 0
h-index: 0
机构:
Natl Def Med Ctr, Grad Inst Life Sci, Taipei, Taiwan
Acad Sinica, Inst Mol Biol, Taipei, Taiwan Natl Def Med Ctr, Grad Inst Life Sci, Taipei, Taiwan

Wu, Huey-Nan
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h-index: 0
机构:
Acad Sinica, Inst Mol Biol, Taipei, Taiwan Natl Def Med Ctr, Grad Inst Life Sci, Taipei, Taiwan
机构:
[1] Natl Def Med Ctr, Grad Inst Life Sci, Taipei, Taiwan
[2] Acad Sinica, Inst Mol Biol, Taipei, Taiwan
关键词:
Dengue virus NS3 protein;
RTPase/ATPase/unwinding activities;
viral RNA replication;
TYPE-2 NONSTRUCTURAL PROTEIN-3;
SINGLE-STRANDED RNA;
CRYSTAL-STRUCTURE;
HELICASE/NUCLEOSIDE TRIPHOSPHATASE;
CATALYTIC DOMAIN;
SERINE-PROTEASE;
NS4B;
RESOLUTION;
5'-TRIPHOSPHATASE;
POLYMERASE;
D O I:
10.1002/1873-3468.12232
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
070307 [化学生物学];
071010 [生物化学与分子生物学];
摘要:
Structure-based mutagenesis analysis on selected conserved surface basic residues of DENV NS3 helicase was performed using a selectable replicon and recombinant protein. We found a requirement for basic side chains of NS3 residues #225, #268, and #538 to activate viral RNA replication and ensure RNA-stimulated ATPase activity, and a critical role for R560 and R599 residues in maintaining NS3 helicase structure, linked to its biological function and catalytic activity. Three screened NS3 second-site mutations for R225A and R268A/E mutations elevated the functional RNA binding of NS3 helicase and compensated the replication defect of the original NS3 mutant replicons.
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收藏
页码:2307 / 2320
页数:14
相关论文
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