STRUCTURE OF A MOUSE IMMUNOGLOBULIN-G THAT LACKS THE ENTIRE CH1 DOMAIN - PROTEIN SEQUENCING AND SMALL-ANGLE X-RAY-SCATTERING STUDIES

The structure of a short-chain IgG2a antibody, which is a member of the family of mouse anti-dansyl switch variant antibodies with identical variable regions but different heavy-chain constant regions [Dangl, J. L., Parks, D. R., Oi, V. T., & Herzenberg, L. A. (1982) Cytometry 2, 395–401], is reported. Amino acid sequencing analyses have demonstrated that in the short-chain IgG2a antibody the entire CH1 domain is deleted whereas the hinge region remains intact. Small-angle X-ray scattering data were collected for the short-chain IgG2a antibody and compared with those for the switch variant IgG1, IgG2a, and IgG2b antibodies with the normal heavy chain. It has been concluded that deletion of the CH1 domain results in a large structural change and the short-chain IgG2a antibody possesses an elongated molecular shape with a much smaller hinge angle as compared with the normal IgG2a antibody that is a Y-shaped molecule. © 1990, American Chemical Society. All rights reserved.