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PDBsum entry 1pd3
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Unknown function
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PDB id
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1pd3
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the m1 protein-Binding domain of the influenza a virus nuclear export protein (nep/ns2).
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Authors
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H.Akarsu,
W.P.Burmeister,
C.Petosa,
I.Petit,
C.W.Müller,
R.W.Ruigrok,
F.Baudin.
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Ref.
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Embo J, 2003,
22,
4646-4655.
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PubMed id
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Abstract
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During influenza virus infection, viral ribonucleoproteins (vRNPs) are
replicated in the nucleus and must be exported to the cytoplasm before
assembling into mature viral particles. Nuclear export is mediated by the
cellular protein Crm1 and putatively by the viral protein NEP/NS2. Proteolytic
cleavage of NEP defines an N-terminal domain which mediates RanGTP-dependent
binding to Crm1 and a C-terminal domain which binds to the viral matrix protein
M1. The 2.6 A crystal structure of the C-terminal domain reveals an amphipathic
helical hairpin which dimerizes as a four-helix bundle. The NEP-M1 interaction
involves two critical epitopes: an exposed tryptophan (Trp78) surrounded by a
cluster of glutamate residues on NEP, and the basic nuclear localization signal
(NLS) of M1. Implications for vRNP export are discussed.
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