The structural requirements for complement activation by IgG: does it hinge on the hinge?

O H Brekke; T E Michaelsen; I Sandlie

doi:10.1016/0167-5699(95)80094-8

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The structural requirements for complement activation by IgG: does it hinge on the hinge?

O H Brekke·T E Michaelsen·I Sandlie

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Abstract

The flexibility of antibody molecules principally derives from the structure of the hinge region. It has generally been accepted that the flexibility of the IgG hinge is necessary for complement activation to occur; however, recent studies dispute this premise. As described here by Ole Henrik Brekke, Terje Michaelsen and Inger Sandlie, it now appears that the only requirement of the hinge region for complement activation is the presence of inter-heavy-chain disulfide bond(s). Furthermore, the structural basis for the differences between IgG subclasses with respect to effector functions appear to be located within the CH2 domain of the immunoglobulin molecule.

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Amino Acid Sequence Animals Complement Activation Humans Immunoglobulin Constant Regions Immunoglobulin G Molecular Sequence Data Protein Conformation Structure-Activity Relationship Journal Article Research Support, Non-U.S. Gov't Review

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O H Brekke, T E Michaelsen, I Sandlie. 1995. The structural requirements for complement activation by IgG: does it hinge on the hinge?. https://doi.org/10.1016/0167-5699(95)80094-8

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