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-Structure paper
Title | Structure of human complement C8, a precursor to membrane attack. |
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Journal, issue, pages | J Mol Biol, Vol. 405, Issue 2, Page 325-330, Year 2011 |
Publish date | Jan 14, 2011 |
![]() | Doryen Bubeck / Pietro Roversi / Rossen Donev / B Paul Morgan / Oscar Llorca / Susan M Lea / ![]() |
PubMed Abstract | Complement component C8 plays a pivotal role in the formation of the membrane attack complex (MAC), an important antibacterial immune effector. C8 initiates membrane penetration and coordinates MAC ...Complement component C8 plays a pivotal role in the formation of the membrane attack complex (MAC), an important antibacterial immune effector. C8 initiates membrane penetration and coordinates MAC pore formation. High-resolution structures of C8 subunits have provided some insight into the function of the C8 heterotrimer; however, there is no structural information describing how the intersubunit organization facilitates MAC assembly. We have determined the structure of C8 by electron microscopy and fitted the C8α-MACPF (membrane attack complex/perforin)-C8γ co-crystal structure and a homology model for C8β-MACPF into the density. Here, we demonstrate that both the C8γ protrusion and the C8α-MACPF region that inserts into the membrane upon activation are accessible. |
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Methods | EM (single particle) |
Resolution | 25.0 Å |
Structure data | ![]() EMDB-1805: |
Source |
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