PDBsum entry 4zdu

Protein transport/signaling protein

PDB id: 4zdu

Contents

Protein chains

416 a.a.

12 a.a.

Waters ×80

PDB id:

4zdu

Name:

Protein transport/signaling protein

Title:

Crystal structure of importin-alpha bound to a non-classical nuclear localization signal of the influenza a virus nucleoprotein

Structure:

Importin subunit alpha-1. Chain: a. Fragment: unp residues 72-498. Synonym: importin alpha p1,karyopherin subunit alpha-2,pendulin,pore targeting complex 58 kda subunit,ptac58,rag cohort protein 1,srp1- alpha. Engineered: yes. Peptide from nucleoprotein. Chain: b.

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: kpna2, rch1. Expressed in: escherichia coli. Expression_system_taxid: 562. Influenza a virus (a/puerto rico/8/1934(h1n1)). Organism_taxid: 211044. Strain: a/puerto rico/8/1934 h1n1.

Resolution:

2.30Å R-factor: 0.191 R-free: 0.246

Authors:

R.Nakada,H.Hirano,Y.Matsuura

Key ref:

R.Nakada et al. (2015). Structure of importin-α bound to a non-classical nuclear localization signal of the influenza A virus nucleoprotein. Sci Rep, 5, 15055. PubMed id: 26456934 DOI: 10.1038/srep15055

Date:

19-Apr-15 Release date: 21-Oct-15

Protein chain

P52293  (IMA1_MOUSE) -  Importin subunit alpha-1 from Mus musculus

Seq: 529 a.a.

Struc: 416 a.a.

Protein chain

P03466  (NCAP_I34A1) -  Nucleoprotein from Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)

Seq: 498 a.a.

Struc: 12 a.a.

DOI no: 10.1038/srep15055

Sci Rep 5:15055 (2015)

PubMed id: 26456934

Structure of importin-α bound to a non-classical nuclear localization signal of the influenza A virus nucleoprotein.

R.Nakada, H.Hirano, Y.Matsuura.

ABSTRACT

A non-classical nuclear localization signal (ncNLS) of influenza A virus nucleoprotein (NP) is critical for nuclear import of viral genomic RNAs that transcribe and replicate in the nucleus of infected cells. Here we report a 2.3 Å resolution crystal structure of mouse importin-α1 in complex with NP ncNLS. The structure reveals that NP ncNLS binds specifically and exclusively to the minor NLS-binding site of importin-α. Structural and functional analyses identify key binding pockets on importin-α as potential targets for antiviral drug development. Unlike many other NLSs, NP ncNLS binds to the NLS-binding domain of importin-α weakly with micromolar affinity. These results suggest that a modest inhibitor with low affinity to importin-α could have anti-influenza activity with minimal cytotoxicity.