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PDBsum entry 4lg2

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protein dna_rna Protein-protein interface(s) links
RNA binding protein/RNA PDB id
4lg2

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
122 a.a.
DNA/RNA
Waters ×8
PDB id:
4lg2
Name: RNA binding protein/RNA
Title: Crystal structure of reston ebola virus vp35 RNA binding domain bound to 12-bp dsrna
Structure: Polymerase cofactor. Chain: a, b, c, d. Fragment: unp residues 205-329. Engineered: yes. Dsrna. Chain: e, f, j, i. Engineered: yes
Source: Reston ebolavirus. Rebov. Organism_taxid: 386032. Strain: reston. Gene: vp35, rebovgp2. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes
Resolution:
2.70Å     R-factor:   0.211     R-free:   0.262
Authors: S.Bale,J.-P.Julien,Z.A.Bornholdt,A.S.Krois,I.A.Wilson,E.O.Saphire
Key ref: S.Bale et al. (2013). Ebolavirus VP35 coats the backbone of double-stranded RNA for interferon antagonism. J Virol, 87, 10385-10388. PubMed id: 23824825 DOI: 10.1128/JVI.01452-13
Date:
27-Jun-13     Release date:   10-Jul-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8JPY0  (VP35_EBORR) -  Polymerase cofactor VP35 from Reston ebolavirus (strain Reston-89)
Seq:
Struc:
329 a.a.
122 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

DNA/RNA chains
  C-U-A-G-A-C-G-U-C 9 bases
  G-A-C-G-U-C-U-A-G 9 bases
  C-U-A-G-A-C-G-U-C-U-A-G 12 bases
  C-U-A-G-A-C-G-U-C-U-A-G 12 bases

 

 
DOI no: 10.1128/JVI.01452-13 J Virol 87:10385-10388 (2013)
PubMed id: 23824825  
 
 
Ebolavirus VP35 coats the backbone of double-stranded RNA for interferon antagonism.
S.Bale, J.P.Julien, Z.A.Bornholdt, A.S.Krois, I.A.Wilson, E.O.Saphire.
 
  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.
 

 

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