Lukoyanova, N. and Hoogenboom, B.W. and Saibil, Helen R. (2016) The membrane attack complex, perforin and cholesterol-dependent cytolysin superfamily of pore-forming proteins. Journal of Cell Science 129 (11), pp. 2125-2133. ISSN 0021-9533.
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Abstract
The membrane attack complex and perforin proteins (MACPFs) and bacterial cholesterol-dependent cytolysins (CDCs) are two branches of a large and diverse superfamily of pore-forming proteins that function in immunity and pathogenesis. During pore formation, soluble monomers assemble into large transmembrane pores through conformational transitions that involve extrusion and refolding of two α-helical regions into transmembrane β-hairpins. These transitions entail a dramatic refolding of the protein structure, and the resulting assemblies create large holes in cellular membranes, but they do not use any external source of energy. Structures of the membrane-bound assemblies are required to mechanistically understand and modulate these processes. In this Commentary, we discuss recent advances in the understanding of assembly mechanisms and molecular details of the conformational changes that occur during MACPF and CDC pore formation.
Metadata
| Item Type: | Article |
|---|---|
| Keyword(s) / Subject(s): | CDC, MACPF, Pore-forming proteins |
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Research Centres and Institutes: | Structural Molecular Biology, Institute of (ISMB) |
| Depositing User: | Administrator |
| Date Deposited: | 13 May 2016 09:39 |
| Last Modified: | 02 Aug 2023 17:23 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/15164 |
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