2FOM
Dengue Virus NS2B/NS3 Protease
Summary for 2FOM
Entry DOI | 10.2210/pdb2fom/pdb |
Descriptor | polyprotein, CHLORIDE ION, GLYCEROL, ... (5 entities in total) |
Functional Keywords | flavivirus, ns3 protease, ns2b cofactor, viral protein-protease complex, viral protein/protease |
Biological source | Dengue virus 2 More |
Cellular location | Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side : Q91H74 Q91H74 |
Total number of polymer chains | 2 |
Total formula weight | 26566.05 |
Authors | Schiering, N.,Kroemer, M.,Renatus, M.,Erbel, P.,D'Arcy, A. (deposition date: 2006-01-13, release date: 2006-03-07, Last modification date: 2024-04-03) |
Primary citation | Erbel, P.,Schiering, N.,D'Arcy, A.,Renatus, M.,Kroemer, M.,Lim, S.P.,Yin, Z.,Keller, T.H.,Vasudevan, S.G.,Hommel, U. Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus. Nat.Struct.Mol.Biol., 13:372-373, 2006 Cited by PubMed Abstract: The replication of flaviviruses requires the correct processing of their polyprotein by the viral NS3 protease (NS3pro). Essential for the activation of NS3pro is a 47-residue region of NS2B. Here we report the crystal structures of a dengue NS2B-NS3pro complex and a West Nile virus NS2B-NS3pro complex with a substrate-based inhibitor. These structures identify key residues for NS3pro substrate recognition and clarify the mechanism of NS3pro activation. PubMed: 16532006DOI: 10.1038/nsmb1073 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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