PDBsum entry 1fbi

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protein Protein-protein interface(s) links
Complex (antibody/antigen) PDB id
Jmol PyMol
Protein chains
214 a.a. *
221 a.a. *
129 a.a. *
* Residue conservation analysis
PDB id:
Name: Complex (antibody/antigen)
Title: Crystal structure of a cross-reaction complex between fab f9.13.7 and guinea-fowl lysozyme
Structure: Igg1 f9.13.7 fab (light chain). Chain: l, p. Engineered: yes. Igg1 f9.13.7 fab (heavy chain). Chain: h, q. Engineered: yes. Guinea fowl lysozyme. Chain: x, y. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Numida meleagris. Helmeted guineafowl. Organism_taxid: 8996
Biol. unit: Trimer (from PQS)
3.00Å     R-factor:   0.190    
Authors: J.Lescar,P.M.Alzari
Key ref: J.Lescar et al. (1995). Crystal structure of a cross-reaction complex between Fab F9.13.7 and guinea fowl lysozyme. J Biol Chem, 270, 18067-18076. PubMed id: 7629116
19-Jan-95     Release date:   27-Feb-95    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P01837  (IGKC_MOUSE) -  Ig kappa chain C region
106 a.a.
214 a.a.
Protein chains
Pfam   ArchSchema ?
P01868  (IGHG1_MOUSE) -  Ig gamma-1 chain C region secreted form
324 a.a.
221 a.a.
Protein chains
Pfam   ArchSchema ?
P00704  (LYSC_NUMME) -  Lysozyme C
129 a.a.
129 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     blood microparticle   5 terms 
  Biological process     metabolic process   10 terms 
  Biochemical function     catalytic activity     6 terms  


J Biol Chem 270:18067-18076 (1995)
PubMed id: 7629116  
Crystal structure of a cross-reaction complex between Fab F9.13.7 and guinea fowl lysozyme.
J.Lescar, M.Pellegrini, H.Souchon, D.Tello, R.J.Poljak, N.Peterson, M.Greene, P.M.Alzari.
The crystal structure of the complex between the cross-reacting antigen Guinea fowl lysozyme and the Fab from monoclonal antibody F9.13.7, raised against hen egg lysozyme, has been determined by x-ray diffraction to 3-A resolution. The antibody interacts with exposed residues of an alpha-helix and surrounding loops adjacent to the lysozyme active site cleft. The epitope of lysozyme bound by antibody F9.13.7 overlaps almost completely with that bound by antibody HyHEL10; the same 12 residues of the antigen interact with the two antibodies. The antibodies, however, have different combining sites with no sequence homology at any of their complementarity-determining regions and show a dissimilar pattern of cross-reactivity with heterologous antigens. Side chain mobility of epitope residues contributes to confer steric and electrostatic complementarity to differently shaped combining sites, allowing functional mimicry to occur. The capacity of two antibodies that have different fine specificities to bind the same area of the antigen emphasizes the operational character of the definition of an antigenic determinant. This example demonstrates that degenerate binding of the same structural motif does not require the existence of sequence homology or other chemical similarities between the different binding sites.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19264660 R.Rajamanonmani, C.Nkenfou, P.Clancy, Y.H.Yau, S.G.Shochat, S.Sukupolvi-Petty, W.Schul, M.S.Diamond, S.G.Vasudevan, and J.Lescar (2009).
On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes.
  J Gen Virol, 90, 799-809.  
18299339 M.Mo, H.C.Lee, M.Kotaka, M.Niang, X.Gao, J.K.Iyer, J.Lescar, and P.Preiser (2008).
The C-terminal segment of the cysteine-rich interdomain of Plasmodium falciparum erythrocyte membrane protein 1 determines CD36 binding and elicits antibodies that inhibit adhesion of parasite-infected erythrocytes.
  Infect Immun, 76, 1837-1847.  
18234071 V.Moreau, C.Fleury, D.Piquer, C.Nguyen, N.Novali, S.Villard, D.Laune, C.Granier, and F.Molina (2008).
PEPOP: computational design of immunogenic peptides.
  BMC Bioinformatics, 9, 71.  
16754878 D.Paus, and G.Winter (2006).
Mapping epitopes and antigenicity by site-directed masking.
  Proc Natl Acad Sci U S A, 103, 9172-9177.  
17145365 R.J.Duquesnoy (2006).
A structurally based approach to determine HLA compatibility at the humoral immune level.
  Hum Immunol, 67, 847-862.  
14988501 A.Cauerhff, F.A.Goldbaum, and B.C.Braden (2004).
Structural mechanism for affinity maturation of an anti-lysozyme antibody.
  Proc Natl Acad Sci U S A, 101, 3539-3544.
PDB code: 1p2c
15034934 G.Johnson, and S.W.Moore (2004).
Functional idiotypic mimicry of an adhesion- and differentiation-promoting site on acetylcholinesterase.
  J Cell Biochem, 91, 999.  
14581222 S.Mohan, N.Sinha, and S.J.Smith-Gill (2003).
Modeling the binding sites of anti-hen egg white lysozyme antibodies HyHEL-8 and HyHEL-26: an insight into the molecular basis of antibody cross-reactivity and specificity.
  Biophys J, 85, 3221-3236.  
12470479 H.Oliva, B.Moltedo, P.De Ioannes, F.Faunes, A.E.De Ioannes, and M.I.Becker (2002).
Monoclonal antibodies to molluskan hemocyanin from Concholepas concholepas demonstrate common and specific epitopes among subunits.
  Hybrid Hybridomics, 21, 365-374.  
12237453 J.Pons, J.R.Stratton, and J.F.Kirsch (2002).
How do two unrelated antibodies, HyHEL-10 and F9.13.7, recognize the same epitope of hen egg-white lysozyme?
  Protein Sci, 11, 2308-2315.  
  11878763 G.Cunto-Amesty, P.Luo, B.Monzavi-Karbassi, and T.Kieber-Emmons (2001).
Exploiting molecular mimicry: defining rules of the game.
  Int Rev Immunol, 20, 157-180.  
10737939 D.W.Ritchie, and G.J.Kemp (2000).
Protein docking using spherical polar Fourier correlations.
  Proteins, 39, 178-194.  
11193052 P.B.Furtado, R.Furmonaviciene, J.McElveen, H.F.Sewell, and F.Shakib (2000).
Prediction of the interacting surfaces in a trimolecular complex formed between the major dust mite allergen Der p 1, a mouse monoclonal anti-Der p 1 antibody, and its anti-idiotype.
  Mol Pathol, 53, 324-332.  
10570132 J.M.van Den Elsen, D.A.Kuntz, F.J.Hoedemaeker, and D.R.Rose (1999).
Antibody C219 recognizes an alpha-helical epitope on P-glycoprotein.
  Proc Natl Acad Sci U S A, 96, 13679-13684.
PDB code: 2ap2
10223295 M.H.Seto, H.L.Liu, D.A.Zajchowski, and M.Whitlow (1999).
Protein fold analysis of the B30.2-like domain.
  Proteins, 35, 235-249.  
  9504719 C.Demangel, S.Rouyre, P.M.Alzari, F.Nato, S.Longacre, P.Lafaye, and J.C.Mazie (1998).
Phage-displayed mimotopes elicit monoclonal antibodies specific for a malaria vaccine candidate.
  Biol Chem, 379, 65-70.  
  9423831 J.P.Bouvet, and G.Dighiero (1998).
From natural polyreactive autoantibodies to à la carte monoreactive antibodies to infectious agents: is it a small world after all?
  Infect Immun, 66, 1-4.  
9186654 G.Dighiero (1997).
Natural autoantibodies, tolerance, and autoimmunity.
  Ann N Y Acad Sci, 815, 182-192.  
9434905 I.A.Wilson, and K.C.Garcia (1997).
T-cell receptor structure and TCR complexes.
  Curr Opin Struct Biol, 7, 839-848.  
8784355 A.Desmyter, T.R.Transue, M.A.Ghahroudi, M.H.Thi, F.Poortmans, R.Hamers, S.Muyldermans, and L.Wyns (1996).
Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme.
  Nat Struct Biol, 3, 803-811.
PDB code: 1mel
8952503 B.A.Fields, F.A.Goldbaum, W.Dall'Acqua, E.L.Malchiodi, A.Cauerhff, F.P.Schwarz, X.Ysern, R.J.Poljak, and R.A.Mariuzza (1996).
Hydrogen bonding and solvent structure in an antigen-antibody interface. Crystal structures and thermodynamic characterization of three Fv mutants complexed with lysozyme.
  Biochemistry, 35, 15494-15503.
PDB codes: 1kip 1kiq 1kir
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.