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PDBsum entry 1fai

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protein Protein-protein interface(s) links
Immunoglobulin PDB id
1fai

 

 

 

 

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Contents
Protein chains
214 a.a.
221 a.a. *
* Residue conservation analysis
PDB id:
1fai
Name: Immunoglobulin
Title: Three-dimensional structure of two crystal forms of fab r19.9, from a monoclonal anti-arsonate antibody
Structure: Igg2b-kappa r19.9 fab (light chain). Chain: l. Engineered: yes. Igg2b-kappa r19.9 fab (heavy chain). Chain: h. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Organism_taxid: 10090
Biol. unit: Dimer (from PQS)
Resolution:
2.70Å     R-factor:   0.189    
Authors: M.B.Lascombe,P.M.Alzari,R.J.Poljak,A.Nisonoff
Key ref: M.B.Lascombe et al. (1992). Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody. Proc Natl Acad Sci U S A, 89, 9429-9433. PubMed id: 1409652 DOI: 10.1073/pnas.89.20.9429
Date:
27-May-92     Release date:   15-Oct-92    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01837  (IGKC_MOUSE) -  Immunoglobulin kappa constant from Mus musculus
Seq:
Struc:
107 a.a.
214 a.a.
Protein chain
No UniProt id for this chain
Struc: 221 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1073/pnas.89.20.9429 Proc Natl Acad Sci U S A 89:9429-9433 (1992)
PubMed id: 1409652  
 
 
Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody.
M.B.Lascombe, P.M.Alzari, R.J.Poljak, A.Nisonoff.
 
  ABSTRACT  
 
The three-dimensional structure of FabR19.9 from a well-characterized anti-p-azobenzenearsonate monoclonal antibody has been determined by x-ray diffraction techniques in two crystalline forms (I and II) to a resolution of 2.8 and 2.7 A, respectively. Essentially the same tertiary and quaternary structure of the Fab is observed in the two forms. The major difference resides in the intermolecular contacts, which are interpreted to favor an irreversible transition from the metastable form I to the more stable form II. The third complementarity-determining region of the heavy chain (H3) folds back over the combining site and requires rearrangement for hapten binding. This dynamic requirement on H3 is consistent with its mobility in the structure and can explain hapten binding to an otherwise inaccessible antibody combining site.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21047817 R.Day, K.P.Lennox, D.B.Dahl, M.Vannucci, and J.W.Tsai (2010).
Characterizing the regularity of tetrahedral packing motifs in protein tertiary structure.
  Bioinformatics, 26, 3059-3066.  
12606718 T.Ota, J.P.Rast, G.W.Litman, and C.T.Amemiya (2003).
Lineage-restricted retention of a primitive immunoglobulin heavy chain isotype within the Dipnoi reveals an evolutionary paradox.
  Proc Natl Acad Sci U S A, 100, 2501-2506.  
10859335 M.Brown, M.A.Schumacher, G.D.Wiens, R.G.Brennan, and M.B.Rittenberg (2000).
The structural basis of repertoire shift in an immune response to phosphocholine.
  J Exp Med, 191, 2101-2112.
PDB code: 1dl7
9370431 J.L.Pellequer, and S.W.Chen (1997).
Does conformational free energy distinguish loop conformations in proteins?
  Biophys J, 73, 2359-2375.  
8870072 P.Bork, A.K.Downing, B.Kieffer, and I.D.Campbell (1996).
Structure and distribution of modules in extracellular proteins.
  Q Rev Biophys, 29, 119-167.  
  9018602 R.R.Joshi (1996).
A self-organizing cognitive network of antibody repertoire development.
  J Comput Biol, 3, 529-545.  
8519975 M.Viswanathan, J.M.Anchin, P.R.Droupadi, C.Mandal, D.S.Linthicum, and S.Subramaniam (1995).
Structural predictions of the binding site architecture for monoclonal antibody NC6.8 using computer-aided molecular modeling, ligand binding, and spectroscopy.
  Biophys J, 69, 741-753.  
7964464 P.J.Johansson, C.Malone, W.Swietnicki, B.M.Dunn, and R.C.Williams (1994).
Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors.
  J Exp Med, 180, 1873-1888.  
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. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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