Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 22, Issue 3, Pages 342-349Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2012.04.008
Keywords
-
Categories
Funding
- NHMRC CDA fellowship
- ARC Discovery project [DP0986811]
- National Institutes of Health NIAID [5R01AI037657-16]
- Australian Research Council [DP0986811] Funding Source: Australian Research Council
Ask authors/readers for more resources
The bacterial cholesterol dependent cytolysins (CDCs) and membrane attack complex/perforin-like proteins (MACPF) represent two major branches of a large, exceptionally diverged superfamily. Most characterized CDC/MACPF proteins form large pores that function in immunity, venoms, and pathogenesis. Extensive structural, biochemical and biophysical studies have started to address some of the questions surrounding how the soluble, monomeric form of these remarkable molecules recognize diverse targets and assemble into oligomeric membrane embedded pores. This review explores mechanistic similarities and differences in how CDCs and MACPF proteins form pores.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available