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PDBsum entry 3hzy

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protein ligands metals Protein-protein interface(s) links
Immune system PDB id
3hzy

 

 

 

 

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Contents
Protein chains
215 a.a. *
219 a.a. *
Ligands
KDA-KDO-KDO
Metals
_ZN ×4
_MG ×2
Waters ×330
* Residue conservation analysis
PDB id:
3hzy
Name: Immune system
Title: Crystal structure of s73-2 antibody in complex with antigen kdo(2.4) kdo(2.4)kdo
Structure: S73-2 fab (igg1k) light chain. Chain: a. S73-2 fab (igg1k) heavy chain. Chain: b
Source: Mus musculus. Mouse. Organism_taxid: 10090. Strain: balb/c. Other_details: ascites. Other_details: ascites
Resolution:
2.10Å     R-factor:   0.219     R-free:   0.261
Authors: C.L.Brooks,S.Muller-Loennies,S.N.Borisova,L.Brade,P.Kosma,T.Hirama, C.R.Mackenzie,H.Brade,S.V.Evans
Key ref: C.L.Brooks et al. (2010). Antibodies raised against chlamydial lipopolysaccharide antigens reveal convergence in germline gene usage and differential epitope recognition. Biochemistry, 49, 570-581. PubMed id: 20000757
Date:
24-Jun-09     Release date:   12-Jan-10    
PROCHECK
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 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 215 a.a.
Protein chain
No UniProt id for this chain
Struc: 219 a.a.
Key:    Secondary structure  CATH domain

 

 
Biochemistry 49:570-581 (2010)
PubMed id: 20000757  
 
 
Antibodies raised against chlamydial lipopolysaccharide antigens reveal convergence in germline gene usage and differential epitope recognition.
C.L.Brooks, S.Müller-Loennies, S.N.Borisova, L.Brade, P.Kosma, T.Hirama, C.R.Mackenzie, H.Brade, S.V.Evans.
 
  ABSTRACT  
 
The structures of antigen-binding fragments from two related monoclonal antibodies have been determined to high resolution in the presence of several carbohydrate antigens raised against chlamydial lipopolysaccharide. With the exception of CDR H3, antibodies S54-10 and S73-2 are both derived from the same set of germline gene segments as the previously reported structures S25-2 and S45-18. Despite this similarity, the antibodies differ in specificity and the mechanism by which they recognize their cognate antigen. S54-10 uses an unrelated CDR H3 to recognize its antigen in a fashion analogous to S45-18; however, S73-2 recognizes the same antigen as S45-18 and S54-10 in a wholly unrelated manner. Together, these antibody-antigen structures provide snapshots into how the immune system uses the same set of inherited germline gene segments to generate multiple possible specificities that allow for differential recognition of epitopes and how unrelated CDR H3 sequences can result in convergent binding of clinically relevant bacterial antigens.
 

 

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