antibody structure

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Introduction to Antibody Structure/Function

• Structure of antibodies (IgG1) • 2x heavy chains (~450 residues) • 2x light chains (~212 residues) • Disulfide bonds (inter & intra chain) • Common terms: • Antigen • Epitope • Paratope • Fab • Fc • Fv • Complementarity determining regions (CDRs) • Framework regions Fv Fc Fab

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Antibody structure and isotypes

Figure 1 Antibody structure and isotypes Antibody isotypes In mammals antibodies are divided into five isotypes: IgG IgM IgA IgD and IgE based on the number of Y units and the type of heavy chain The isotypes differ in their biological properties functional locations and ability to deal with different antigens: Heavy chains

What is the Y shape of an antibody?
The top of the Y shape contains the variable region, which binds tightly and specifically to an epitope on the antigen. The light chains of an antibody can be classified as either kappa (κ) or lambda (λ) type based on small differences in polypeptide sequence. The heavy chain makeup determines the overall class of each antibody (Figure 1).
What are the functional components of an intact antibody molecule?
The intact antibody molecule shown in Figure 1has three functional components, two Fragment antigen binding domains (Fabs) and the fragment crystallizable (Fc), with the two Fabs linked to the Fc by a hinge region that allows the Fabs a large degree of conformation flexibility relative to the Fc.

Antibodies: Structures types and functions

Antibody structure and function Immunoglobulin

Detailed Antibody Structure (FL-Immuno/35)

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