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Five different cholesterol-dependent cytolysins (CDCs) have now had their atomic structures solved. Here their structures are compared and shown to vary less in the C-terminal region than they do in their N-terminal MACPF/CDC homology region. The most variable region of the C-terminal domain is the undecapeptide, which is observed in two clusters of conformations, and comparison of this domain with the C2 domain of perforin shows that the two structures have a common ancestor. Structural studies of CDC pre-pore and pore oligomers by cryo-electron microscopy and atomic force microscopy have revealed much about their mechanism of action. Understanding the activity of CDCs has required a combination of structural, biophysical and functional assays but current models of pore formation still require development to account for variable functional pore size.

Original publication

DOI

10.1007/978-94-017-8881-6_4

Type

Journal article

Journal

Subcell Biochem

Publication Date

2014

Volume

80

Pages

47 - 62

Keywords

Animals, Cholesterol, Complement Membrane Attack Complex, Cytotoxins, Humans, Models, Molecular, Perforin, Phylogeny, Polymerization, Protein Conformation