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C8 alpha and C8 beta have correspondingly similar roles in MAC-mediated lysis of erythrocytes and bacterial killing. C8 gamma is not required for complement-mediated killing of Gram-negative bacteria.
The binding specificity between C8 alpha and C8 beta subunits is determined by a cooperative interaction of the N-terminal thrombospondin type 1 module and the membrane attack complex/perforin (show PRF1 Proteins) domain.
Both N-terminal modules in C8 alpha have a role in forming the principal binding site for C9, and binding may be dependent on a cooperative interaction between these modules and the C8 alpha membrane attack complex/perforin (show PRF1 Proteins) domain.
result suggests that this segment of C8alpha and corresponding segments of the other MAC family members are independently folded domains
C8 is a component of the complement system and contains three polypeptides, alpha, beta and gamma. This gene encodes the alpha subunit of C8. C8 participates in the formation of the membrane attack complex (MAC). The MAC assembles on bacterial membranes to form a pore, permitting disruption of bacterial membrane organization. Mutations in this gene cause complement C8 alpha-gamma deficiency.
complement component 8 subunit alpha
, complement component C8 alpha chain
, complement component 8 alpha subunit
, complement component C8 alpha subunit