4CO6

Crystal structure of the Nipah virus RNA free nucleoprotein- phosphoprotein complex

Summary for 4CO6

• Entry DOI: 10.2210/pdb4co6/pdb
• Descriptor: NUCLEOPROTEIN, PHOSPHOPROTEIN, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: chaperone, viral protein, viral replication, paramyxovirus
• Biological source: NIPAH VIRUS; More
• Cellular location: Virion: Q9IK92 Q9IK91
• Total number of polymer chains: 6
• Total formula weight: 139790.43

Authors

Yabukarksi, F.,Lawrence, P.,Tarbouriech, N.,Bourhis, J.M.,Jensen, M.R.,Ruigrok, R.W.H.,Blackledge, M.,Volchkov, V.,Jamin, M. (deposition date: 2014-01-27, release date: 2014-08-13, Last modification date: 2024-10-23)

Primary citation

Yabukarksi, F.,Lawrence, P.,Tarbouriech, N.,Bourhis, J.M.,Delaforge, E.,Jensen, M.R.,Ruigrok, R.W.H.,Blackledge, M.,Volchkov, V.,Jamin, M.
Structure of Nipah Virus Unassembled Nucleoprotein in Complex with its Viral Chaperone.
Nat.Struct.Mol.Biol., 21:754-, 2014

PubMed Abstract: Nipah virus (NiV) is a highly pathogenic emergent paramyxovirus causing deadly encephalitis in humans. Its replication requires a constant supply of unassembled nucleoprotein (N(0)) in complex with its viral chaperone, the phosphoprotein (P). To elucidate the chaperone function of P, we reconstituted NiV the N(0)-P core complex and determined its crystal structure. The binding of the N-terminal region of P blocks the polymerization of N by interfering with subdomain exchange between N protomers and keeps N(0) in an open conformation, ready to grasp an RNA molecule. We found that a peptide derived from the N-binding region of P protects cells against viral infection and demonstrated by structure-based mutagenesis that this peptide acts by inhibiting N(0)-P formation. These results provide new insights about the assembly of N along genomic RNA and validate the N(0)-P complex as a target for drug development.

PubMed: 25108352
DOI: 10.1038/NSMB.2868

Experimental method

X-RAY DIFFRACTION (2.498 Å)