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PDBsum entry 12e8

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protein Protein-protein interface(s) links
Immunoglobulin PDB id
12e8

 

 

 

 

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Contents
Protein chains
214 a.a. *
221 a.a. *
Waters ×767
* Residue conservation analysis
PDB id:
12e8
Name: Immunoglobulin
Title: 2e8 fab fragment
Structure: Igg1-kappa 2e8 fab (light chain). Chain: l, m. Fragment: fab fragment. Igg1-kappa 2e8 fab (heavy chain). Chain: h, p. Fragment: fab fragment
Source: Mus musculus. House mouse. Organism_taxid: 10090. Strain: balb/c. Cell_line: 2e8 hybridoma. Organ: spleen. Cell: lymphocyte-plasma cell. Cell: lymphocyte-plasma cell
Biol. unit: Dimer (from PQS)
Resolution:
1.90Å     R-factor:   0.221     R-free:   0.271
Authors: B.Rupp,S.Trakhanov
Key ref:
S.Trakhanov et al. (1999). Structure of a monoclonal 2E8 Fab antibody fragment specific for the low-density lipoprotein-receptor binding region of apolipoprotein E refined at 1.9 A. Acta Crystallogr D Biol Crystallogr, 55, 122-128. PubMed id: 10089402 DOI: 10.1107/S090744499800938X
Date:
14-Mar-98     Release date:   05-Aug-98    
PROCHECK
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 Headers
 References

Protein chains
No UniProt id for this chain
Struc: 214 a.a.
Protein chains
No UniProt id for this chain
Struc: 221 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1107/S090744499800938X Acta Crystallogr D Biol Crystallogr 55:122-128 (1999)
PubMed id: 10089402  
 
 
Structure of a monoclonal 2E8 Fab antibody fragment specific for the low-density lipoprotein-receptor binding region of apolipoprotein E refined at 1.9 A.
S.Trakhanov, S.Parkin, R.Raffaï, R.Milne, Y.M.Newhouse, K.H.Weisgraber, B.Rupp.
 
  ABSTRACT  
 
The crystal structure of the Fab fragment of 2E8, the monoclonal IgG1,kappa antibody specific for the low-density lipoprotein (LDL) receptor-binding region of apolipoprotein E (apoE), has been solved by molecular replacement and refined at 1.9 A resolution (PDB entry 12E8). Two 2E8 Fab molecules in the asymmetric unit are related by noncrystallographic symmetry and are hydrogen bonded through a beta-sheet-like intermolecular contact between the heavy-chain complementarity-determining regions 3 (CDRH3) of each molecule. The structure has been refined to an R value of 0.22 (Rfree = 0.27). The initially ill-defined heavy-chain constant domain (CH1) of 2E8 has been retraced with the aid of automatic refinement, confirming the beta-sheet tracing independently of any starting models. As a resolution better than 2 A is not common for Fab fragments, this model represents a well defined Fab structure and should prove useful in MR solution of other Fab fragments. Furthermore, in the absence of an LDL-receptor structure, the homology of the 2E8 CDRH2 to the ligand-binding domain of the LDL receptor has been exploited to model the apoE-LDL-receptor interaction.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 Native Patterson map created by XtalView (McRee, 1992[McRee, D. E. (1992). J. Mol. Graph. 10, 44-46.]) showing the strong Harker peak indicative of an NCS axis parallel to the crystallographic 2[1] screw axis.
Figure 4.
Figure 4 Ribbon representation of the topology of the 2E8 Fab dimer. The two light chains (C[L] and V[L]) are red and yellow, respectively, and the two heavy chains (C[H1] and V[H]) are blue and green, respectively. The dimer interface is formed by the complementarity-determining regions. The figure was created with MOLSCRIPT (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]).
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 122-128) copyright 1999.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference Google scholar

  PubMed id Reference
19136675 A.Honegger, A.D.Malebranche, D.Röthlisberger, and A.Plückthun (2009).
The influence of the framework core residues on the biophysical properties of immunoglobulin heavy chain variable domains.
  Protein Eng Des Sel, 22, 121-134.  
  10850798 B.W.Segelke, M.Forstner, M.Knapp, S.D.Trakhanov, S.Parkin, Y.M.Newhouse, H.D.Bellamy, K.H.Weisgraber, and B.Rupp (2000).
Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: implications for lipid binding.
  Protein Sci, 9, 886-897.
PDB codes: 1bz4 1or2 1or3
10702278 R.Raffaï, K.H.Weisgraber, R.MacKenzie, B.Rupp, E.Rassart, T.Hirama, T.L.Innerarity, and R.Milne (2000).
Binding of an antibody mimetic of the human low density lipoprotein receptor to apolipoprotein E is governed through electrostatic forces. Studies using site-directed mutagenesis and molecular modeling.
  J Biol Chem, 275, 7109-7116.  
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 codes are shown on the right.

 

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