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通过结构域插入工程化变构蛋白开关。

Engineering allosteric protein switches by domain insertion.

作者信息

Ostermeier Marc

机构信息

Department of Chemical and Biomolecular Engineering, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD 21218, USA.

出版信息

Protein Eng Des Sel. 2005 Aug;18(8):359-64. doi: 10.1093/protein/gzi048. Epub 2005 Jul 25.

DOI:10.1093/protein/gzi048
PMID:16043448
Abstract

Domain insertion is proving to be an effective way to construct hybrid proteins exhibiting switch-like behavior. In this strategy, two existing domains, the first exhibiting a signal recognition function and the second containing the function to be modulated, are fused such that the recognition of the signal by the first domain is transmitted to the second domain, thereby modulating its activity. Recent directed evolution experiments indicate that the structural space comprised of the recombination of unrelated protein domains may be rich in switching behavior, particularly when the circular permutation of domains is also employed. This bodes well for potential basic science, sensing and therapeutic applications of molecular switches.

摘要

结构域插入已被证明是构建具有开关样行为的杂合蛋白的有效方法。在这种策略中,将两个现有的结构域融合,第一个结构域具有信号识别功能,第二个结构域包含待调节的功能,使得第一个结构域对信号的识别传递到第二个结构域,从而调节其活性。最近的定向进化实验表明,由不相关蛋白质结构域重组构成的结构空间可能富含开关行为,特别是当也采用结构域的环形排列时。这对于分子开关在潜在的基础科学、传感和治疗应用方面是个好兆头。

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