2FP7

West Nile Virus NS2B/NS3protease in complex with Bz-Nle-Lys-Arg-Arg-H

Summary for 2FP7

• Entry DOI: 10.2210/pdb2fp7/pdb
• Related: 2FOM
• Related PRD ID: PRD_000988
• Descriptor: Genome polyprotein, N-benzoyl-L-norleucyl-L-lysyl-N-[(2S)-5-carbamimidamido-1-hydroxypentan-2-yl]-L-argininamide, ... (4 entities in total)
• Functional Keywords: flavivirus, ns3 protease, ns2b cofactor, substrate-based inhibitor, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: West Nile virus (WNV); More
• Cellular location: Capsid protein C: Virion . Peptide pr: Secreted . Small envelope protein M: Virion membrane ; Multi-pass membrane protein . Envelope protein E: Virion membrane ; Multi-pass membrane protein . Non-structural protein 1: Secreted . Non-structural protein 2A: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Multi-pass membrane protein . Serine protease NS3: Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side . Non-structural protein 4A: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Non-structural protein 4B: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side : P06935 P06935
• Total number of polymer chains: 3
• Total formula weight: 25353.52

Authors

Schiering, N.,D'Arcy, A.,Erbel, P. (deposition date: 2006-01-16, 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

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

Experimental method

X-RAY DIFFRACTION (1.68 Å)