PDBsum entry 1aif

Go to PDB code: 
protein Protein-protein interface(s) links
Immunoglobulin PDB id
Protein chains
215 a.a. *
218 a.a. *
* Residue conservation analysis
PDB id:
Name: Immunoglobulin
Title: Anti-idiotypic fab 409.5.3 (igg2a) fab from mouse
Structure: Anti-idiotypic fab 409.5.3 (igg2a) fab (light chain). Chain: l, a. Anti-idiotypic fab 409.5.3 (igg2a) fab (heavy chain). Chain: h, b
Source: Mus musculus. House mouse. Organism_taxid: 10090. Organism_taxid: 10090
Biol. unit: Dimer (from PQS)
2.90Å     R-factor:   0.220    
Authors: N.Ban,C.Escobar,K.Hasel,J.Day,A.Greenwood,A.Mcpherson
Key ref: N.Ban et al. (1995). Structure of an anti-idiotypic Fab against feline peritonitis virus-neutralizing antibody and a comparison with the complexed Fab. FASEB J, 9, 107-114. PubMed id: 7821749
14-Nov-94     Release date:   01-Feb-97    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P01837  (IGKC_MOUSE) -  Ig kappa chain C region
106 a.a.
215 a.a.
Protein chains
No UniProt id for this chain
Struc: 218 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     plasma membrane   1 term 
  Biochemical function     antigen binding     1 term  


FASEB J 9:107-114 (1995)
PubMed id: 7821749  
Structure of an anti-idiotypic Fab against feline peritonitis virus-neutralizing antibody and a comparison with the complexed Fab.
N.Ban, C.Escobar, K.W.Hasel, J.Day, A.Greenwood, A.McPherson.
The crystal structure of anti-idiotopic Fab 409.5.3, made against an E2 specific feline infectious peritonitis virus-neutralizing antibody 730.1.4, has been determined in its free from, at 2.9 A resolution by molecular replacement. This antibody, used as an immmunogen, elicits the production of anti-anti-idiotypic antibodies that in turn neutralize the virus. The structure of the uncomplexed Fab was refined using constrained-restrained least squares minimization and simulated annealing in combination with conjugate gradient techniques to a crystallographic R of 0.22 based on 16,482 unique reflections between 20.0 and 2.9 A. The free antiidiotypic Fab shows, when compared to its complexed form, a 5 degrees rotation of its variable light with respect to its variable heavy domain and rearrangement of complementarity determining region loops, which permits optimization of the stereocomplementarity between interacting molecules. This finding supports the induced fit hypothesis for antibody antigen interaction.

Literature references that cite this PDB file's key reference

  PubMed id Reference
12743303 J.F.Conway, N.R.Watts, D.M.Belnap, N.Cheng, S.J.Stahl, P.T.Wingfield, and A.C.Steven (2003).
Characterization of a conformational epitope on hepatitis B virus core antigen and quasiequivalent variations in antibody binding.
  J Virol, 77, 6466-6473.  
10737939 D.W.Ritchie, and G.J.Kemp (2000).
Protein docking using spherical polar Fourier correlations.
  Proteins, 39, 178-194.  
10585914 B.Carrasco, la Torre, O.Byron, D.King, C.Walters, S.Jones, and S.E.Harding (1999).
Novel size-independent modeling of the dilute solution conformation of the immunoglobulin IgG Fab' domain using SOLPRO and ELLIPS.
  Biophys J, 77, 2902-2910.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.