Abstract
Membrane attack by complement involves the self-assembly on membranes of five hydrophilic proteins (C5b, C6, C7, C8 and C9) to an amphiphilic tubular complex comprising approximately 20 subunits. The hydrophilic-amphiphilic transition of the precursor proteins is achieved by restricted unfolding and exposure of previously hidden hydrophobic domains. Restricted unfolding, in turn, is driven by high-affinity protein-protein interactions resulting in the formation of amphilic complexes. Circular polymerization of C9 to a tubular complex (poly C9) constitutes the molecular mechanism for transmembrane channel assembly and formation of ultrastructural membrane lesions.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 589-603 |
| Number of pages | 15 |
| Journal | Molecular Immunology |
| Volume | 21 |
| Issue number | 7 |
| DOIs | |
| State | Published - Jul 1984 |
ASJC Scopus subject areas
- Immunology
- Molecular Biology
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Cite this
Podack, E. R., & Tschopp, J. (1984). Membrane attack by complement. Molecular Immunology, 21(7), 589-603. https://doi.org/10.1016/0161-5890(84)90044-0