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PDBsum entry 2fp7
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Hydrolase/hydrolase inhibitor
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PDB id
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2fp7
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References listed in PDB file
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Key reference
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Title
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Structural basis for the activation of flaviviral ns3 proteases from dengue and west nile virus.
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Authors
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P.Erbel,
N.Schiering,
A.D'Arcy,
M.Renatus,
M.Kroemer,
S.P.Lim,
Z.Yin,
T.H.Keller,
S.G.Vasudevan,
U.Hommel.
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Ref.
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Nat Struct Mol Biol, 2006,
13,
372-373.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Figure 1. Structures of NS2B–NS3pro in the absence and
presence of an inhibitor. (a) DEN NS2B–NS3pro. Gray,
NS3pro; yellow, NS2B. No electron density was observed for NS2B
residues 77–84. (b) WNV NS2B–NS3pro in complex with
Bz-Nle-Lys-Arg-Arg-H (orange). Residue numbering is according to
Supplementary Figure 2. Figures were made in PyMOL
(http://pymol.sourceforge.net/).
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Figure 2.
Figure 2. Stereo view of the substrate-binding region of WNV
NS2B–NS3pro, colored as in Figure 1. Potential hydrogen
bonds are indicated (dotted lines).
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2006,
13,
372-373)
copyright 2006.
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