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Structure of IDP05773

Structural Basis of Type-I Interferon Sequestration by a Poxvirus Decoy Receptor

Edit deposit information
CSGID target
IDP05773 
PDB Id
3OQ3 (NCBI MMDB
Authors
D.H.Fremont,C.A.Lee,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Chris Nelson 
Responsible lab
Washington University 
Deposition Date
Sep 02, 2010 
Release Date
May 18, 2011 

Annotation

Description
Poxvirus have evolved an array of mechanisms to circumvent the effects of type I interferons (IFNs), a group of cytokines known for their ability to confer resistance to viral infection. For example, the virulent rodent pathogen Ectromelia virus, that causes mousepox, encodes a secreted decoy receptor named EVM166 that is able to bind and inhibit type-I INFs. This entry contains a crystal structure of EVM166 in complex with murine IFNα5 and reveals a striking similarity between EVM166 and the ectodomain of the human receptor for IL-1β. The regions buried by EVM166 on IFNα5 are thought to be crucial for its’ interactions with the host-encoded INF-α receptor (a cell-surface heterodimer consisting of the two chains IFNAR1 and IFNAR2). Many species within the orthopoxvirus genus encode decoy receptors for type-I INFs that have sequence similarity to EVM166. These include Vaccinia, Cowpox, and Variola, among others. Sub-species that lack or encode truncated versions of EVM166 display a significantly attenuated phenotype in mice demonstrating the importance of this decoy receptor as a virulence factor. The information contained in this entry may prove useful in the future development of antiviral therapeutics targeted against poxviruses. It may also prove useful in the design and creation of novel anti-inflammatory therapeutics.  
Functional assignment
virulence factor 

Ligands

Ligand code Name Ligand type
EPE
CL
ACT
EDO
ZN ZINC ION

Structure information

Unit cell parameters

Space Group
P 21 21 21  
Unit Cell

a=48.84Å, b=75.90Å, c=182.73Å
α=90.00, β=90.00, γ=90.00 
Solvent content
 
Matthews coefficient
 

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
43.07-2.10Å (2.18-2.10Å)  
Rall(%)
20.4 
Rwork(%)
20.3 (0.0) 
Rfree(%)
23.5 (0.0) 
Num. observed reflections
71824 (7650) 
Num. Rfree reflections
3519 (382) 
Completeness(%)
95.9 (92.5) 

Model parameters

Num Atoms
3974  
Num Waters
1  
Num Hetatoms
417  
Model mean isotropic B factor
35.890Å2  
RMSD bond length
0.000Å  
RMSD bond angle
0.000°  
Filename uploaded
pdb_extract_coord_15251.cif (uploaded on Sep 13, 2010 4:21 PM)  
Inserted
Sep 13, 2010