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The membrane attack complex, perforin and cholesterol-dependent cytolysin superfamily of pore-forming proteins

Lukoyanova, N; Hoogenboom, BW; Saibil, HR; (2016) The membrane attack complex, perforin and cholesterol-dependent cytolysin superfamily of pore-forming proteins. Journal of Cell Science , 129 (11) pp. 2125-2133. 10.1242/jcs.182741. Green open access

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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.

Type: Article
Title: The membrane attack complex, perforin and cholesterol-dependent cytolysin superfamily of pore-forming proteins
Open access status: An open access version is available from UCL Discovery
DOI: 10.1242/jcs.182741
Publisher version: http://dx.doi.org/10.1242/jcs.182741
Language: English
Additional information: Copyright © 2016 The author. Published by The Company of Biologists Ltd. The published article is available at
Keywords: CDC; MACPF; Pore-forming proteins
UCL classification: UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences > Dept of Physics and Astronomy
URI: https://discovery.ucl.ac.uk/id/eprint/1493829
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