Dynamic Aspects of the Immunoglobulin Structure.
Immunoglobulin (Ig) molecules are composed of Fab and Fc portions tethered by a hinge region that enables them to rotate and flex, relative to each other. Variable (V) and constant (C) domains of the Fab are connected by a flexible elbow region that is responsible for the movements of the V and C heterodimers. Significant movements of Fc domains have also been documented. The Ig portion's rotational freedom greatly enhances its ability to react with antigens and cell receptors, often simultaneously. The antigen-combining site also displays a dynamic structure. The ability of its various parts to change position greatly facilitates their complexation with various antigenic compounds.
['Nezlin|Roald|R|']
D000941:Antigens D006801:Humans D007140:Immunoglobulin Fab Fragments D007141:Immunoglobulin Fc Fragments D007074:Immunoglobulin G D008958:Models, Molecular D011485:Protein Binding D000072417:Protein Domains D055503:Protein Multimerization D012399:Rotation
Fab elbow angle Immunoglobulin flexibility combining site flexibility glycan residue movements intrinsic domain flexibility mobility of Fab and Fc domains