Structure of the Malpha2-3 toxin alpha antibody-antigen complex: combination of modelling with functional mapping experimental results.
Modelled structures of the acetylcholine receptor-mimicking antibody, Malpha2-3, both free and bound to its antigen, toxin alpha, are assessed in the light of new experimental mutational data from functional mapping of the paratopic region of Malpha2-3. The experimental results are consistent with the previously-predicted structure of the free antibody, and also demonstrate that structural particularities of the Malpha2-3 combining site that were identified in the models play a role in the protein association. The modelled conformations of the hypervariable loops are discussed in the context of recent new data and analyses. The new mutational data allow several previously-considered modelled structures of the complex to be rejected. Two quite similar models now remain.
Tenette-Souaille
C
C
Section de Biophysique des Prot¿eines et des Membranes, DBCM, CEN-Saclay, 91191 Gif-sur-Yvette, France.
Smith
J C
JC
D000906:Antibodies / Q000737:chemistry*; D018604:Epitope Mapping; D008958:Models, Molecular; D011487:Protein Conformation; D011950:Receptors, Cholinergic / Q000276:immunology*; D014118:Toxins, Biological / Q000276:immunology*
D000906:Antibodies; D011950:Receptors, Cholinergic; D014118:Toxins, Biological