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Domain Structure of an Antibody (IgG 1)

click on any of the domains for a CHIME 3D-display of the structure, or select from the list on the right
The comparison of the IgG2a structure (PDB entry 1igt) and the IgG1structure (PDB entry 1igy) demonstrates the flexibility of the hinge region: The two structures are drawn with the same orientation of the FC fragment, but the Fab fragments point in different directions in the two crystal structures. This flexibility renders crystallization of entire antibody molecules very difficult. Most of the antibody structures in the PDB database are structures of Fab fragments. Homogenous preparations of Fab fragments can be obtained from monoclonal antibodies by limited digestion with the protease papain. Digestion with pepsin yields (Fab)2-fragments, which retain part of the hinge region.
Individual domains, Fv-fragments and Fab fragments can also be produced as recombinant proteins in E.coli. Here, the single-chain Fv format is frequently used: a VL and a VH domain are connected by a flexible peptide linker of about 15 amino acids length. Shorter linker lengths may lead to diabody formation as the linker is too short to allow correct domain pairing in a single molecule.
entire IgG1 molecule
Fab2-Fragment
Fab-Fragment
Fv-Fragment
Hinge
FC-Fragment
VL-Domain
CL-Domain
VH-Domain
CH-Domain
CH2-Domain
CH3-Domain
AAAAA Homepage Zürich University Dept. of Biochemistry Plückthun Group Annemarie Honegger

Last Modified by A.Honegger Tuesday, January 25, 2005