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Dynamic Aspects of the Immunoglobulin Structure

Roald Nezlin1

  • 1Department of Immunology, The Weizmann Institute of Science , Rehovot , Israel.

Immunological Investigations
|May 3, 2019
PubMed

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.

Keywords:
Fab elbow angleImmunoglobulin flexibilitycombining site flexibilityglycan residue movementsintrinsic domain flexibilitymobility of Fab and Fc domains

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