4LG2

Crystal structure of Reston Ebola virus VP35 RNA binding domain bound to 12-bp dsRNA

Summary for 4LG2

• Entry DOI: 10.2210/pdb4lg2/pdb
• Related: 3FKE 3KS8 3L25 3L26 4GHA
• Descriptor: Polymerase cofactor, dsRNA (3 entities in total)
• Functional Keywords: rna binding domain, dsrna binding protein, dsrna, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Reston ebolavirus (REBOV)
• Cellular location: Virion: Q8JPY0
• Total number of polymer chains: 8
• Total formula weight: 81505.73

Authors

Bale, S.,Julien, J.-P.,Bornholdt, Z.A.,Krois, A.S.,Wilson, I.A.,Saphire, E.O. (deposition date: 2013-06-27, release date: 2013-07-10, Last modification date: 2023-09-20)

Primary citation

Bale, S.,Julien, J.P.,Bornholdt, Z.A.,Krois, A.S.,Wilson, I.A.,Saphire, E.O.
Ebolavirus VP35 coats the backbone of double-stranded RNA for interferon antagonism.
J.Virol., 87:10385-10388, 2013

PubMed Abstract: Recognition of viral double-stranded RNA (dsRNA) activates interferon production and immune signaling in host cells. Crystal structures of ebolavirus VP35 show that it caps dsRNA ends to prevent sensing by pattern recognition receptors such as RIG-I. In contrast, structures of marburgvirus VP35 show that it primarily coats the dsRNA backbone. Here, we demonstrate that ebolavirus VP35 also coats the dsRNA backbone in solution, although binding to the dsRNA ends probably constitutes the initial binding event.

PubMed: 23824825
DOI: 10.1128/JVI.01452-13

Experimental method

X-RAY DIFFRACTION (2.7 Å)