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PDBsum entry 3j2y

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protein Protein-protein interface(s) links
Immune system PDB id
3j2y

 

 

 

 

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Contents
Protein chains
212 a.a.
218 a.a.
PDB id:
3j2y
Name: Immune system
Title: Electron cryo-microscopy of chikungunya vlp in complex with neutralizing antibody fab 9.8b
Structure: 9.8b light chain. Chain: a, c, e, g. Fragment: fab. 9.8b heavy chain. Chain: b, d, f, h. Fragment: fab
Source: Mus musculus. Mouse. Organism_taxid: 10090. Organism_taxid: 10090
Authors: S.Sun,Y.Xiang,M.G.Rossmann
Key ref: S.Sun et al. (2013). Structural analyses at pseudo atomic resolution of Chikungunya virus and antibodies show mechanisms of neutralization. Elife, 2, e00435. PubMed id: 23577234 DOI: 10.7554/eLife.00435
Date:
28-Jan-13     Release date:   24-Apr-13    
PROCHECK
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 Headers
 References

Protein chains
No UniProt id for this chain
Struc: 212 a.a.
Protein chains
No UniProt id for this chain
Struc: 218 a.a.
Key:    Secondary structure

 

 
DOI no: 10.7554/eLife.00435 Elife 2:e00435 (2013)
PubMed id: 23577234  
 
 
Structural analyses at pseudo atomic resolution of Chikungunya virus and antibodies show mechanisms of neutralization.
S.Sun, Y.Xiang, W.Akahata, H.Holdaway, P.Pal, X.Zhang, M.S.Diamond, G.J.Nabel, M.G.Rossmann.
 
  ABSTRACT  
 
A 5.3 Å resolution, cryo-electron microscopy (cryoEM) map of Chikungunya virus-like particles (VLPs) has been interpreted using the previously published crystal structure of the Chikungunya E1-E2 glycoprotein heterodimer. The heterodimer structure was divided into domains to obtain a good fit to the cryoEM density. Differences in the T = 4 quasi-equivalent heterodimer components show their adaptation to different environments. The spikes on the icosahedral 3-fold axes and those in general positions are significantly different, possibly representing different phases during initial generation of fusogenic E1 trimers. CryoEM maps of neutralizing Fab fragments complexed with VLPs have been interpreted using the crystal structures of the Fab fragments and the VLP structure. Based on these analyses the CHK-152 antibody was shown to stabilize the viral surface, hindering the exposure of the fusion-loop, likely neutralizing infection by blocking fusion. The CHK-9, m10 and m242 antibodies surround the receptor-attachment site, probably inhibiting infection by blocking cell attachment. DOI:http://dx.doi.org/10.7554/eLife.00435.001.
 

 

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