Clusterin binds C5b-C7, C8, C9

Stable Identifier
Reaction [binding]
Homo sapiens
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Clusterin is a dimer of two fragments of the same translation product, which are disulfide bonded by five cysteines on each peptide (Tobe et al. 1991). It is able to modulate the terminal complement cascade in vitro and prevent cellular lysis by the membrane attack complex (MAC), C5b-9. Clusterin forms complexes with C5b:C6:C7, or C5b:C6:C7:C8 or C5b:C6:C7:C8:C9, as the proteins assemble into the amphiphilic MAC. Clusterin binding renders the complexes soluble and lytically inactive (Jenne & Tschopp 1989, Choi et al. 1989, Murphy et al. 1989, Tschopp et al. 1993).

Literature References
PubMed ID Title Journal Year
8345200 Clusterin, the human apolipoprotein and complement inhibitor, binds to complement C7, C8 beta, and the b domain of C9

Tschopp, J, Chonn, A, Hertig, S, French, LE

J. Immunol. 1993
Participant Of
Orthologous Events
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