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Lookup NU author(s): Professor Jeremy LakeyORCiD
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Membrane disruption can efficiently alter cellular function; indeed, pore-forming toxins (PFTs) are well known as important bacterial virulence factors. However, recent data have revealed that structures similar to those found in PFTs are found in membrane active proteins across disparate phyla. Many similarities can be identified only at the 3D-structural level. Of note, domains found in membrane-attack complex proteins of complement and perforin (MACPF) resemble cholesterol-dependent cytolysins from Gram-positive bacteria, and the Bcl family of apoptosis regulators share similar architectures with Escherichia coli pore-forming colicins. These and other correlations provide considerable help in understanding the structural requirements for membrane binding and pore formation. © 2008 Elsevier Ltd. All rights reserved.
Author(s): Anderluh G, Lakey JH
Publication type: Review
Publication status: Published
Journal: Trends in Biochemical Sciences
Year: 2008
Volume: 33
Issue: 10
Pages: 482-490
ISSN (print): 0968-0004
ISSN (electronic): 0167-7640
URL: http://dx.doi.org/10.1016/j.tibs.2008.07.004
DOI: 10.1016/j.tibs.2008.07.004
