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Protein topology and allostery.
Current Opinion in Structural Biology ( IF 6.1 ) Pub Date : 2020-02-14 , DOI: 10.1016/j.sbi.2020.01.011
Juan Xie 1 , Luhua Lai 2
Affiliation  

Allostery plays important roles in many biological processes. Although all non-fibrous proteins may be allosteric, currently only a limited number of allosteric proteins are known. How allosteric regulation depends on protein topology and what are the preferred folds in allosteric proteins need to be explored. Allosteric sites are found more often between chains or domains in multimeric or multi-domain proteins, while they often occur on the opposite side of the structure of the protein from the orthosteric site in monomeric single domain proteins. Although most folds are found in allosteric proteins, the immunoglobulin-like fold is rarely used. Typical regulatory domains include alpha-beta plaits, PDZ, WW domains, and so on. According to the understandings of allosteric regulations, novel allosteric proteins and materials have been rationally designed.

中文翻译:

蛋白质拓扑和变构。

变构在许多生物过程中起着重要作用。尽管所有非纤维蛋白都可能是变构的,但目前只有有限数量的变构蛋白是已知的。变构调节如何取决于蛋白质拓扑结构以及变构蛋白质中的首选折叠是什么,需要探索。变构位点更常见于多聚体或多域蛋白质中的链或域之间,而它们通常出现在蛋白质结构的与单体单域蛋白质中的正构位点相反的一侧。尽管在变构蛋白中发现了大多数折叠,但很少使用免疫球蛋白样折叠。典型的调控域包括 alpha-beta 辫子、PDZ、WW 域等。根据变构规律的理解,
更新日期:2020-02-14
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