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Disparate proteins use similar architectures to damage membranes

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.

Publication metadata

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


DOI: 10.1016/j.tibs.2008.07.004