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Disparate proteins use similar architectures to damage membranes

Disparate proteins use similar architectures to damage membranes

Authors :
Gregor Anderluh
Jeremy H. Lakey
Source :
Trends in Biochemical Sciences. 33:482-490
Publication Year :
2008
Publisher :
Elsevier BV, 2008.

Abstract

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.

Details

ISSN :
09680004
Volume :
33
Database :
OpenAIRE
Journal :
Trends in Biochemical Sciences
Accession number :
edsair.doi.dedup.....1bcb766a5b87a88d759aeb3ba7915696
Full Text :
https://doi.org/10.1016/j.tibs.2008.07.004