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PDBsum entry 2vq1

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protein ligands Protein-protein interface(s) links
Immune system PDB id
2vq1

 

 

 

 

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Contents
Protein chains
217 a.a.
213 a.a. *
Ligands
GLY ×8
GOL ×3
AZI
Waters ×214
* Residue conservation analysis
PDB id:
2vq1
Name: Immune system
Title: Anti trimeric lewis x fab54-5c10-a
Structure: Igkv1-117 protein. Chain: a, e. Synonym: fab54-5c10-a. Other_details: antigen binding fragment. Anti-human fc gamma receptor iii 3g8 gamma heavy chain variable region. Chain: b, f. Synonym: fab54-5c10-a. Other_details: antigen binding fragment
Source: Mus musculus. Mouse. Organism_taxid: 10090. Strain: swiss. Cell_line: murine hybridoma. Cell_line: murine hybridoma
Resolution:
2.50Å     R-factor:   0.206     R-free:   0.260
Authors: D.C.De Geus,A.M.M.Van Roon,E.A.J.Thomassen,C.H.Hokke,A.M.Deelder, J.P.Abrahams
Key ref: D.C.de Geus et al. (2009). Characterization of a diagnostic Fab fragment binding trimeric Lewis X. Proteins, 76, 439-447. PubMed id: 19173313
Date:
10-Mar-08     Release date:   27-Jan-09    
PROCHECK
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 Headers
 References

Protein chains
No UniProt id for this chain
Struc: 217 a.a.
Protein chains
No UniProt id for this chain
Struc: 213 a.a.
Key:    Secondary structure  CATH domain

 

 
Proteins 76:439-447 (2009)
PubMed id: 19173313  
 
 
Characterization of a diagnostic Fab fragment binding trimeric Lewis X.
D.C.de Geus, A.M.van Roon, E.A.Thomassen, C.H.Hokke, A.M.Deelder, J.P.Abrahams.
 
  ABSTRACT  
 
Lewis X trisaccharides normally function as essential cell-cell interaction mediators. However, oligomers of Lewis X trisaccharides expressed by the parasite Schistosoma mansoni seem to be related to its evasion of the immune response of its human host. Here we show that monoclonal antibody 54-5C10-A, which is used to diagnose schistosomiasis in humans, interacts with oligomers of at least three Lewis X trisaccharides, but not with monomeric Lewis X. We describe the sequence and the 2.5 A crystal structure of its Fab fragment and infer a possible mode of binding of the polymeric Lewis X from docking studies. Our studies indicate a radically different mode of binding compared to Fab 291-2G3-A, which is specific for monomeric Lewis X, thus providing a structural explanation of the diagnostic success of 54-5C10-A.
 

 

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