Crystal structures of full length DENV4 NS2B-NS3 reveal the dynamic interaction between NS2B and NS3.

We report the crystal structures of linked and unlinked NS2B47-NS3 constructs in their free state and in complex with bovine pancreatic trypsin inhibitor (BPTI). These structures demonstrate that the NS2B cofactor predominantly adopts a closed conformation in complex with full-length NS3. The glycine-rich linker between NS2B and NS3 may promote the open conformation which interferes with protease activity. This negative impact on the enzyme structure and function is restricted to the protease activity as the ATPase activity is not affected in vitro. PMID: 32763315 [PubMed - as supplied by publisher]

https://www.ncbi.nlm.nih.gov/pubmed/32763315?dopt=Abstract

Source: Antiviral Research - August 3, 2020 Category: Virology Authors: Phoo WW, El Sahili A, Zhang Z, Chen MW, Liew CW, Lescar J, Vasudevan SG, Luo D Tags: Antiviral Res Source Type: research