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2FOM

Dengue Virus NS2B/NS3 Protease

Summary for 2FOM
Entry DOI10.2210/pdb2fom/pdb
Descriptorpolyprotein, CHLORIDE ION, GLYCEROL, ... (5 entities in total)
Functional Keywordsflavivirus, ns3 protease, ns2b cofactor, viral protein-protease complex, viral protein/protease
Biological sourceDengue virus 2
More
Cellular locationHost endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side : Q91H74 Q91H74
Total number of polymer chains2
Total formula weight26566.05
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 citationErbel, 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: 16532006
DOI: 10.1038/nsmb1073
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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