The evolution of flexibility and function in the Fc domains of IgM, IgY, and IgE.

ABSTRACT:

Introduction

Antibody Fc regions harbour the binding sites for receptors that mediate effector functions following antigen engagement by the Fab regions. An extended "hinge" region in IgG allows flexibility between Fab and Fc, but in both the most primitive antibody, IgM, and in the evolutionarily more recent IgE, the hinge is replaced by an additional domain pair in the homodimeric six-domain Fc region. This permits additional flexibility within the Fc region, which has been exploited by nature to modulate antibody effector functions. Thus, in pentameric or hexameric IgM, the Fc regions appear to adopt a planar conformation in solution until antigen binding causes a conformational change and exposes the complement binding sites. In contrast, IgE-Fc principally adopts an acu

SUBMITTER: Calvert RA 

PROVIDER: S-EPMC11496790 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature