1pd3

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spinqualitylabelsall models 1pd3, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Influenza A NEP M1-binding domain

Overview

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.

About this Structure

1PD3 is a Single protein structure of sequence from Influenza a virus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)., Akarsu H, Burmeister WP, Petosa C, Petit I, Muller CW, Ruigrok RW, Baudin F, EMBO J. 2003 Sep 15;22(18):4646-55. PMID:12970177

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