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The oligomerization domain of C4b-binding protein (C4BP) is a short C-terminal region found in the alpha chain of this complement inhibitor. It is essential for the formation of the characteristic multimeric (typically heptameric) assembly of C4BP, which is stabilized by intermolecular disulfide bridges between conserved cysteine residues. This architecture is crucial for the full-length C4BP's ability to inhibit the classical and lectin pathways of complement activation. The domain has become a tool in biotechnological applications, where fusion proteins containing the oligomerization domain can improve valency, stability, and half-life of reagents used in immunology and vaccine research.
Not a direct drug target; fusion proteins containing this domain have been engineered to extend half-life or enhance immunogenicity of recombinant proteins.
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