Structure of human complement C8, a precursor to membrane attack
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...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
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2011
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| _version_ | 1797072547180707840 |
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| author | Bubeck, D Roversi, P Donev, R Morgan, B Llorca, O Lea, S |
| author_facet | Bubeck, D Roversi, P Donev, R Morgan, B Llorca, O Lea, S |
| author_sort | Bubeck, D |
| collection | OXFORD |
| description | 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. © 2010 Elsevier Ltd. All rights reserved. |
| first_indexed | 2024-03-06T23:09:17Z |
| format | Journal article |
| id | oxford-uuid:64e78dcb-95e5-4dcd-bb1a-619d5a522c20 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:09:17Z |
| publishDate | 2011 |
| record_format | dspace |
| spelling | oxford-uuid:64e78dcb-95e5-4dcd-bb1a-619d5a522c202022-03-26T18:21:58ZStructure of human complement C8, a precursor to membrane attackJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:64e78dcb-95e5-4dcd-bb1a-619d5a522c20EnglishSymplectic Elements at Oxford2011Bubeck, DRoversi, PDonev, RMorgan, BLlorca, OLea, SComplement 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. © 2010 Elsevier Ltd. All rights reserved. |
| spellingShingle | Bubeck, D Roversi, P Donev, R Morgan, B Llorca, O Lea, S Structure of human complement C8, a precursor to membrane attack |
| title | Structure of human complement C8, a precursor to membrane attack |
| title_full | Structure of human complement C8, a precursor to membrane attack |
| title_fullStr | Structure of human complement C8, a precursor to membrane attack |
| title_full_unstemmed | Structure of human complement C8, a precursor to membrane attack |
| title_short | Structure of human complement C8, a precursor to membrane attack |
| title_sort | structure of human complement c8 a precursor to membrane attack |
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