ArticleBiophysical journal2010
Conformational stability of hepatitis C virus NS3 protease.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- Repurposing Drugs as Bacteroides fragilis BFT-3 Inhibitors in the Animal Infection Model Galleria mellonella.Annals of the New York Academy of Sciences · 2026Article
- Varying molecular interactions explain aspects of crowder-dependent enzyme function of a viral protease.PLoS computational biology · 2023Article
- Repositioning small molecule drugs as allosteric inhibitors of the BFT-3 toxin from enterotoxigenic Bacteroides fragilis.Protein science : a publication of the Protein Society · 2022Article
- Crowding affects structural dynamics and contributes to membrane association of the NS3/4A complex.Biophysical journal · 2021Article
- Flexible Proteins at the Origin of Life.Life (Basel, Switzerland) · 2017Article
- Rescuing compound bioactivity in a secondary cell-based screening by using γ-cyclodextrin as a molecular carrier.International journal of nanomedicine · 2015Article
- A 3D structural model and dynamics of hepatitis C virus NS3/4A protease (genotype 4a, strain ED43) suggest conformational instability of the catalytic triad: implications in catalysis and drug resistivity.Journal of biomolecular structure & dynamics · 2014Article
- pH-dependent conformational changes in the HCV NS3 protein modulate its ATPase and helicase activities.PloS one · 2014Article
- Article
- Post-translational modifications of hepatitis C viral proteins and their biological significance.World journal of gastroenterology · 2013Review
- NS3 protease from hepatitis C virus: biophysical studies on an intrinsically disordered protein domain.International journal of molecular sciences · 2013Review
- Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The hepatitis C virus NS3 protease is responsible for the processing of the nonstructural region of viral precursor polyprotein in infected hepatic cells. NS3 has been considered a target for drug discovery for a long time. NS3 is a zinc-dependent serine protease. However, the zinc ion is not involved in the catalytic mechanism, because it is bound far away from the active site. Thus, zinc is essential for the structural integrity of the protein and it is considered to have a structural role. The first thermodynamic study on the conformational equilibrium and stability of NS3 and the effect of zinc on such equilibrium is presented here. In agreement with a previous calorimetric study on the binding of zinc to NS3, the global unfolding heat capacity is dominated by the zinc dissociation step, suggesting that the binding of zinc induces a significant structural rearrangement of the protein. In addition, contrary to other homologous zinc-dependent proteases, the zinc-free NS3 protease is not completely unstructured. It is apparent that the conformational landscape of hepatitis C virus NS3 protease is fairly complex due to its intrinsic plasticity, and to the interactions with its different effectors (zinc and the accessory viral protein NS4A) and their modulation of the population of the different conformational states.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.