Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 405, Issue 2, Pages 325-330Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2010.10.031
Keywords
C8; complement; 3D electron microscopy; terminal pathway; membrane attack complex (MAC)
Categories
Funding
- MRC, UK [G0400775]
- Wellcome Trust [068590, RGP39/2008]
- Fundacion Ramon Areces, the Spanish Ministry of Science and Innovation [SAF2008-00451]
- Red Tematica de Investigacion Cooperativa en Cancer (RTICC), Instituto de Salud Carlos III [RD06/0020/1001]
- Human Frontiers Science Program
- EMBO
- CRI
- SJC
- MRC [G0700102, G0400775] Funding Source: UKRI
- Medical Research Council [G0400775, G0700102] Funding Source: researchfish
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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 C8 alpha-MACPF (membrane attack complex/perforin)-C8 gamma co-crystal structure and a homology model for C8 beta-MACPF into the density. Here, we demonstrate that both the C8 gamma protrusion and the C8 alpha-MACPF region that inserts into the membrane upon activation are accessible. (C) 2010 Elsevier Ltd. All rights reserved.
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