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Dive into the research topics where Dingjiang Liu is active.

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Featured researches published by Dingjiang Liu.


Protein Science | 2003

Double-stranded DNA-induced localized unfolding of HCV NS3 helicase subdomain 2

Dingjiang Liu; William T. Windsor; Daniel F. Wyss

The NS3 helicase of the hepatitis C virus (HCV) unwinds double‐stranded (ds) nucleic acid (NA) in an NTP‐dependent fashion. Mechanistic details of this process are, however, largely unknown for the HCV helicase. We have studied the binding of dsDNA to an engineered version of subdomain 2 of the HCV helicase (d2ΔNS3h) by NMR and circular dichroism. Binding of dsDNA to d2ΔNS3h induces a local unfolding of helix (α3), which includes residues of conserved helicase motif VI (Q460RxxRxxR467), and strands (β1 and β8) from the central β‐sheet. This also occurs upon lowering the pH (4.4) and introducing an R461A point mutation, which disrupt salt bridges with Asp 412 and Asp 427 in the protein structure. NMR studies on d2ΔNS3h in the partially unfolded state at low pH map the dsDNA binding site to residues previously shown to be involved in single‐stranded DNA binding. Sequence alignment and structural comparison suggest that these Arg–Asp interactions are highly conserved in SF2 DEx(D/H) proteins. Thus, modulation of these interactions by dsNA may allow SF2 helicases to switch between conformations required for helicase function.


Magnetic Resonance in Chemistry | 2004

Competition STD NMR for the detection of high-affinity ligands and NMR-based screening

Yu-Sen Wang; Dingjiang Liu; Daniel F. Wyss


Journal of the American Chemical Society | 2004

Sequence-Specific Assignments of Methyl Groups in High-Molecular Weight Proteins

Daiwen Yang; Yu Zheng; Dingjiang Liu; Daniel F. Wyss


Journal of Molecular Biology | 2001

Solution structure and backbone dynamics of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase

Dingjiang Liu; Yu-Sen Wang; Jennifer J. Gesell; Daniel F. Wyss


Journal of Biomolecular NMR | 2003

Letter to the Editor: Solution structure of the hypothetical protein YqgF from Escherichia coli reveals an RNAse H fold

Dingjiang Liu; Yu-Sen Wang; Daniel F. Wyss


Journal of Biomolecular NMR | 2003

Solution structure of the hypothetical protein YqgF from Escherichia coli reveals an RNAse H fold.

Dingjiang Liu; Yu-Sen Wang; Daniel F. Wyss


Protein Engineering | 2001

Design, high-level expression, purification and characterization of soluble fragments of the hepatitis C virus NS3 RNA helicase suitable for NMR-based drug discovery methods and mechanistic studies

Jennifer J. Gesell; Dingjiang Liu; Vincent S. Madison; Thomas Hesson; Yu-Sen Wang; Patricia C. Weber; Daniel F. Wyss


Journal of Biomolecular NMR | 2004

Letter to the Editor: Backbone Resonance Assignments of the 45.3 kDa Catalytic Domain of Human BACE1

Dingjiang Liu; Yu-Sen Wang; Jennifer J. Gesell; Eileen Wilson; Brian M. Beyer; Daniel F. Wyss


Journal of Biomolecular NMR | 2001

Letter to the Editor: Backbone 1H, 15N and 13C resonance assignments of the NTPase subdomain of the hepatitis C virus NS3 RNA helicase

Dingjiang Liu; Daniel F. Wyss


Journal of Biomolecular NMR | 2000

Letter to the Editor: Sequence-specific 1H, 15N and 13C resonance assignments for an engineered arginine-rich domain of the hepatitis C virus NS3 RNA helicase

Dingjiang Liu; Daniel F. Wyss

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