ArticleProtein science : a publication of the Protein Society1999
Conformational changes in the NS3 protease from hepatitis C virus strain Bk monitored by limited proteolysis and mass spectrometry.
Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Discovery of new molecular entities able to strongly interfere with Hsp90 C-terminal domain.Scientific reports · 2018Article
- Protein Structural Analysis via Mass Spectrometry-Based Proteomics.Advances in experimental medicine and biology · 2016Review
- Mass Spectrometric Analysis of Surface-Exposed Regions in the Hexadecameric Phosphorylase Kinase Complex.Biochemistry · 2015Article
- Article
- Ribosomal protein L7a binds RNA through two distinct RNA-binding domains.The Biochemical journal · 2005Article
- Conformational analysis of HAMLET, the folding variant of human alpha-lactalbumin associated with apoptosis.Protein science : a publication of the Protein Society · 2004Article
- Binding and relaxometric properties of heme complexes with cyanogen bromide fragments of human serum albumin.Biophysical journal · 2002Article
- Topological investigation of amyloid fibrils obtained from beta2-microglobulin.Protein science : a publication of the Protein Society · 2002Article
- The effect of prime-site occupancy on the hepatitis C virus NS3 protease structure.Protein science : a publication of the Protein Society · 2002Article
- Conformational analysis of putative regulatory subunit D of the toluene/o-xylene-monooxygenase complex from Pseudomonas stutzeri OX1.Protein science : a publication of the Protein Society · 2001Article
- Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation.Protein science : a publication of the Protein Society · 2000Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conformational changes occurring within the NS3 protease domain from the hepatitis C virus Bk strain (NS3(1-180)) under different physico-chemical conditions either in the absence or in the presence of its cofactor Pep4A were investigated by limited proteolysis experiments. Because the surface accessibility of the protein is affected by conformational changes, when comparative experiments were carried out on NS3(1-180) either at different glycerol concentrations or in the presence of Pep4A, differential peptide maps were obtained from which protein regions involved in the structural changes could be inferred. The surface topology of isolated NS3(1-180) in solution was essentially consistent with the crystal structure of the protein with the N-terminal segment showing a high conformational flexibility. At higher glycerol concentration, the protease assumed a more compact structure showing a decrease in the accessibility of the N-terminal segment that either was forced to interact with the protein or originate intermolecular interactions with neighboring molecules. Binding of the cofactor Pep4A caused the displacement of the N-terminal arm from the protein moiety, leading this segment to again adopt an open and flexible conformation, thus suggesting that the N-terminus of the protease contributes only marginally to the stability of the complex. The observed conformational changes might be directly correlated with the activation mechanism of the protease by either the cosolvent or the cofactor peptide because they lead to tighter packing of the substrate binding site.
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