Journal
FEBS LETTERS
Volume 588, Issue 14, Pages 2206-2211Publisher
WILEY
DOI: 10.1016/j.febslet.2014.05.018
Keywords
Bovine pancreatic trypsin inhibitor; Dengue virus protease; Lanthanide tag; NMR spectroscopy; Pseudocontact shift
Funding
- government of the People's Republic of China for a CSC scholarship
- Studienstiftung des deutschen Volkes for a fellowship
- Australian Research Council
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The C-terminal p-hairpin of NS2B (NS2Bc) in the dengue virus NS2B-NS3 protease is required for full enzymatic activity. In crystal structures without inhibitor and in the complex with bovine pancreatic trypsin inhibitor (BPTI), NS2Bc is displaced from the active site. In contrast, nuclear magnetic resonance (NMR) studies in solution only ever showed NS2Bc in the enzymatically active closed conformation. Here we demonstrate by pseudocontact shifts from a lanthanide tag that NS2Bc remains in the closed conformation also in the complex with BPTI. Therefore, the closed conformation is the best template for drug discovery. Structured summary of protein interactions: NS2B, BPTI and NS3 physically interact by nuclear magnetic resonance (View interaction) (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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