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Disparate proteins use similar architectures to damage membranes
Disparate proteins use similar architectures to damage membranes
- 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.
- Subjects :
- Models, Molecular
Pore Forming Cytotoxic Proteins
Protein Conformation
Molecular Sequence Data
Biology
medicine.disease_cause
Biochemistry
Drug Stability
Lectins
medicine
Animals
Humans
Amino Acid Sequence
Molecular Biology
Escherichia coli
MACPF
Membranes
Sequence Homology, Amino Acid
biology.organism_classification
Cell biology
Membrane
Perforin
Bacterial virulence
Colicin
biology.protein
Sequence Alignment
Function (biology)
Bacteria
Protein Binding
Subjects
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