Abstract
C3 is the most prominent of the acute-phase complement components. C3 synthesis is tissue-specific and is modulated in response to a variety of stimulatory agents. C3 is synthesized as a prepro single-chain molecule of 1663 amino acids including a 22 amino acid leader peptide and a four amino acid cleavage site. C3 has a two-domain shape, consisting of a flat ellipsoid about 18 nm long, 2 nm thick and 8-10 nm wide, with a smaller flat domain of 2 × 4 × 9 nm, confirmed by scattering solution analysis. The larger domain represents the C3c and the smaller is the C3d region. On proteolytic activation and removal of C3a, there takes place a large conformational change with the two domains moving closer together.
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