1PD3: Influenza A Nep M1-Binding Domain

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.
PDB ID: 1PD3Download
MMDB ID: 25682
PDB Deposition Date: 2003/5/19
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Similar Structures:
Biological Unit for 1PD3: monomeric; determined by author
Molecular Components in 1PD3
Label Count Molecule
Protein (1 molecule)
Nonstructural Protein NS2(Gene symbol: NEP)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB