Disparate proteins use similar architectures to damage membranes.
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.
Anderluh
Gregor
G
Department of Biology, Biotechnical Faculty, University of Ljubljana, Vecna pot 111, 1000, Ljubljana, Slovenia. gregor.anderluh@bf.uni-lj.si
Lakey
Jeremy H
JH
D000595:Amino Acid Sequence; D000818:Animals; D004355:Drug Stability; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000633:toxicity; D008566:Membranes / Q000737:chemistry / Q000187:drug effects*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D052899:Pore Forming Cytotoxic Proteins / Q000737:chemistry* / Q000633:toxicity*; D011485:Protein Binding; D011487:Protein Conformation; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D037102:Lectins; D052899:Pore Forming Cytotoxic Proteins