Antiidiotype complexes

A number of anti-idiotype complexes have been reported (Table 1). However, the lack of availability of the structure of the original antibody in complex with antigen has limited the ability to describe mimicry of the antigen by the idiotypic antibody. In the case of the D1.3 antibody, whose structures both uncomplexed and in complex with antigen (lysozyme) have been determined, two anti-idiotypic complex structures have also been determined. One (E225) blocks the antigen-binding site, but does not

Figure 2 Comparison of complexed and uncomplexed forms of 50.1 showing the change of the binding pocket between the uncomplexed and complexed forms. (A) Superposition of VL domains of 50.1, showing changes due to differences between relative position of VH and conformational differences of the third CDR loop of the heavy chain (complexed antibody in black and uncomplexed antibody in white). (B) Binding site (as represented by a dot surface) of complexed form of 50.1. (C) Binding site (as represented by a dot surface) of uncomplexed form of 50.1. The third CDR of the heavy chain is towards the top center of the figures. (Figure produced with MOLSCRIPT by Per Kraulis.)

mimic the surface of the antigen. In contrast, the other (E5.2) blocks the antigen-binding site and appears to mimic the interactions of lysozvme with D1.3 to a high degree.

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