2fp7

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

Structural highlights

2fp7 is a 3 chain structure with sequence from West nile virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:, ,
Related:2fom
Activity:Flavivirin, with EC number 3.4.21.91
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus.,Erbel P, Schiering N, D'Arcy A, Renatus M, Kroemer M, Lim SP, Yin Z, Keller TH, Vasudevan SG, Hommel U Nat Struct Mol Biol. 2006 Apr;13(4):372-3. Epub 2006 Mar 12. PMID:16532006[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Erbel P, Schiering N, D'Arcy A, Renatus M, Kroemer M, Lim SP, Yin Z, Keller TH, Vasudevan SG, Hommel U. Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus. Nat Struct Mol Biol. 2006 Apr;13(4):372-3. Epub 2006 Mar 12. PMID:16532006 doi:10.1038/nsmb1073

2fp7, resolution 1.68Å

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OCA