6I3H
Crystal structure of influenza A virus M1 N-terminal domain (G18A mutation)
Summary for 6I3H
| Entry DOI | 10.2210/pdb6i3h/pdb |
| Descriptor | Matrix protein 1, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | matrix protein 1 n-terminal domain g18a mutation, viral protein |
| Biological source | Influenza A virus |
| Total number of polymer chains | 2 |
| Total formula weight | 39255.14 |
| Authors | Miyake, Y.,Keusch, J.J.,Decamps, L.,Ho-Xuan, H.,Iketani, S.,Gut, H.,Kutay, U.,Helenius, A.,Yamauchi, Y. (deposition date: 2018-11-06, release date: 2019-09-18, Last modification date: 2024-01-24) |
| Primary citation | Miyake, Y.,Keusch, J.J.,Decamps, L.,Ho-Xuan, H.,Iketani, S.,Gut, H.,Kutay, U.,Helenius, A.,Yamauchi, Y. Influenza virus uses transportin 1 for vRNP debundling during cell entry. Nat Microbiol, 4:578-586, 2019 Cited by PubMed Abstract: Influenza A virus is a pathogen of great medical impact. To develop novel antiviral strategies, it is essential to understand the molecular aspects of virus-host cell interactions in detail. During entry, the viral ribonucleoproteins (vRNPs) that carry the RNA genome must be released from the incoming particle before they can enter the nucleus for replication. The uncoating process is facilitated by histone deacetylase 6 (ref.). However, the precise mechanism of shell opening and vRNP debundling is unknown. Here, we show that transportin 1, a member of the importin-β family proteins, binds to a PY-NLS sequence motif close to the amino terminus of matrix protein (M1) exposed during acid priming of the viral core. It promotes the removal of M1 and induces disassembly of vRNP bundles. Next, the vRNPs interact with importin-α/β and enter the nucleus. Thus, influenza A virus uses dual importin-βs for distinct steps in host cell entry. PubMed: 30692667DOI: 10.1038/s41564-018-0332-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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