Concerning the axial rotational flexibility of the Fab regions of immunoglobulin G.
By electron microscopy, we have observed immunocomplexes with both negative stain and in amorphous ice using monoclonal antibodies directed against one of the 24 subunits of scorpion haemocyanin. A copy of this subunit occurs at each of the corners of the square-shaped haemocyanin molecule. Three distinct orientations of adjacent haemocyanin molecules may be observed in immunocomplex pairs or chains using both the above-mentioned methods. These observations, coupled with low-resolution computer simulations of immunocomplex formation, argue strongly in favour of the existence of a considerable degree of rotational flexibility within the IgG molecule and around the long axis of the Fab arms, as was suggested by previous observations with negative stain. We find that the arms can rotate by up to 180 degrees with respect to the Fc region.
Wade
R H
RH
Laboratoire de Biologie Structurale, LBio-Département de Recherche Fondamentale, CENG, Grenoble, France.
Taveau
J C
JC
Lamy
J N
JN
D000818:Animals; D000936:Antigen-Antibody Complex; D006433:Hemocyanins; D007140:Immunoglobulin Fab Fragments; D007074:Immunoglobulin G; D008854:Microscopy, Electron; D008958:Models, Molecular; D012605:Scorpions
D000936:Antigen-Antibody Complex; D007140:Immunoglobulin Fab Fragments; D007074:Immunoglobulin G; D006433:Hemocyanins