9WA5
Crystal structure of an inactive form of NS2B-NS3 Protease
Summary for 9WA5
| Entry DOI | 10.2210/pdb9wa5/pdb |
| Descriptor | Serine protease subunit NS2B,Serine protease NS3, MAGNESIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | zika virus, viral protease, ns2b-ns3, viral protein |
| Biological source | Zika virus More |
| Total number of polymer chains | 2 |
| Total formula weight | 45245.50 |
| Authors | |
| Primary citation | Ngo, K.H.,Lattmann, S.,Anindita, P.D.,Liew, C.W.,Harris, R.S.,Luo, D.,Kang, C. An inactive Zika NS2B-NS3pro protease construct for investigating allosteric inhibitors. J.Struct.Biol., 218:108314-108314, 2026 Cited by PubMed Abstract: The Zika virus protease, composed of the cofactor region from NS2B and the N-terminal region of NS3, plays a critical role in viral polyprotein maturation and represents an attractive therapeutic target. However, developing small-molecule inhibitors for its highly hydrophilic active site remains challenging, highlighting the importance of pursuing allosteric inhibition strategies. In this study, we engineered an NS2B-NS3 protease containing an 18-residue NS2B sequence linked to the N-terminal region of NS3 via a glycine-rich linker. We determined its crystal structure and obtained the solution NMR spectrum with backbone resonance assigned. This new construct was used in fragment screening and two new fragments were identified. This design excludes the C-terminal part of NS2B cofactor region, whose conformation is influenced by substrate or inhibitor binding, making the construct particularly valuable for screening and characterizing allosteric inhibitors. PubMed: 41833763DOI: 10.1016/j.jsb.2026.108314 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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