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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.
Results describe the crystal structure of the human C8 alpha MACPF domain disulfide-linked to C8 gamma (alphaMACPF-gamma) at 2.15 A resolution.
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 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 domain.
result suggests that this segment of C8alpha and corresponding segments of the other MAC family members are independently folded domains
One can predict that the indel segment of C8alpha assumes a conformation that allows for multiple points of contact with C8gamma.
crystal structure of the MACPF domain of complement component C8alpha at 2.5 angstrom resolution was determined and it was shown that it is structurally homologous to the bacterial, pore-forming, cholesterol-dependent cytolysins
C8gamma binds an indel peptide of C8alpha sequence and forms a non-covalent complex.
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