1PD3

Influenza A NEP M1-binding domain

Summary for 1PD3

• Entry DOI: 10.2210/pdb1pd3/pdb
• Descriptor: Nonstructural protein NS2 (1 entity in total)
• Functional Keywords: influenza virus a, nep/ns2, unknown function
• Biological source: Influenza A virus
• Cellular location: Virion (Potential): P03508
• Total number of polymer chains: 2
• Total formula weight: 14482.50

Authors

Baudin, F. (deposition date: 2003-05-19, release date: 2003-12-16, Last modification date: 2024-02-14)

Primary citation

Akarsu, H.,Burmeister, W.P.,Petosa, C.,Petit, I.,Muller, C.W.,Ruigrok, R.W.,Baudin, F.
Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2).
Embo J., 22:4646-4655, 2003

PubMed Abstract: 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.

PubMed: 12970177
DOI: 10.1093/emboj/cdg449

Experimental method

X-RAY DIFFRACTION (2.6 Å)