期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1858, 期 3, 页码 475-486出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2015.11.017
关键词
MACPF; CDC; Pore forming toxin; Perforin; Membrane Attack Complex; Pleurotolysin
资金
- Monash University FMNHS Postgraduate Bridging Fellowship Award
- Australian Research Council (ARC) [DP120104058, CE140100011]
- National Health and Medical Research Council (NHMRC) [606471]
- ARC
- NHMRC [DP120104058, CE140100011, FF0883418]
- Australian Research Council [FF0883418] Funding Source: Australian Research Council
Pore Forming Toxins (PFTs) represent a key mechanism for permitting the passage of proteins and small molecules across the lipid membrane. These proteins are typically produced as soluble monomers that self-assemble into ring-like oligomeric structures on the membrane surface. Following such assembly PFTs undergo a remarkable conformational change to insert into the lipid membrane. While many different protein families have independently evolved such ability, members of the Membrane Attack Complex PerForin/Cholesterol Dependent Cytolysin (MACPF/CDC) superfamily form distinctive giant beta-barrel pores comprised of up to 50 monomers and up to 300 angstrom in diameter. In this review we focus on recent advances in understanding the structure of these giant MACPF/CDC pores as well as the underlying molecular mechanisms leading to their formation. Commonalities and evolved variations of the pore forming mechanism across the superfamily are discussed. This article is part of a Special Issue entitled: Pore-Forming Toxins edited by Mauro Dalla Serra and Franco Gambale. (C) 2015 Elsevier B.V. All rights reserved.
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