期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 70, 期 12, 页码 2083-2098出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-012-1153-8
关键词
MACPF domain; Cholesterol-dependent cytolysins; Pore; Membrane interactions; Membrane damage
资金
- Oxford Division of Structural Biology is part of the Wellcome Trust Centre for Human Genetics, Wellcome Trust Core Award [090532/Z/09]
- Nanosmart project from the Provincia Autonoma di Trento
- Slovenian Research Agency
Recent work on the MACPF/CDC superfamily of pore-forming proteins has focused on the structural analysis of monomers and pore-forming oligomeric complexes. We set the family of proteins in context and highlight aspects of their function which the direct and exclusive equation of oligomers with pores fails to explain. Starting with a description of the distribution of MACPF/CDC proteins across the domains of life, we proceed to show how their evolutionary relationships can be understood on the basis of their structural homology and re-evaluate models for pore formation by perforin, in particular. We furthermore highlight data showing the role of incomplete oligomeric rings (arcs) in pore formation and how this can explain small pores generated by oligomers of proteins belonging to the family. We set this in the context of cell biological and biophysical data on the proteins' function and discuss how this helps in the development of an understanding of how they act in processes such as apicomplexan parasites gliding through cells and exiting from cells.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据