Pore-forming protein toxins: from structure to function

被引:363
|
作者
Parker, MW [1 ]
Feil, SC [1 ]
机构
[1] St Vincents Inst Med Res, Biota Struct Biol Lab, Fitzroy, Vic 3065, Australia
来源
基金
英国医学研究理事会;
关键词
channels; crystal structures; cytolysins; membrane insertion; pore-forming toxins;
D O I
10.1016/j.pbiomolbio.2004.01.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Pore-forming protein toxins (PFTs) are one of Nature's most potent biological weapons. An essential feature of their toxicity is the remarkable property that PFTs can exist either in a stable water-soluble state or as an integral membrane pore. In order to convert from the water-soluble to the membrane state. the toxin must undergo large conformational changes. There are now more than a dozen PFTs for which crystal structures have been determined and the nature of the conformational changes they must undergo is beginning to be understood. Although they differ markedly in their primary, secondary. tertiary and quaternary structures, nearly all can be classified into one of two families based on the types of pores they are thought to form: alpha-PFTs or beta-PFTs. Recent work suggests a number of common features in the mechanism of membrane insertion may exist for each class. (C) 2004 Elsevier Ltd. All rights reserved.
引用
收藏
页码:91 / 142
页数:52
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