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蛋白质拓扑结构与变构。

Protein topology and allostery.

机构信息

Center for Quantitative Biology, Peking University, Beijing 100871, China.

BNLMS, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China; Center for Quantitative Biology, Peking University, Beijing 100871, China; Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China.

出版信息

Curr Opin Struct Biol. 2020 Jun;62:158-165. doi: 10.1016/j.sbi.2020.01.011. Epub 2020 Feb 14.

Abstract

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.

摘要

变构作用在许多生物过程中起着重要作用。虽然所有非纤维蛋白都可能具有变构作用,但目前已知的变构蛋白数量有限。变构调节如何依赖于蛋白质拓扑结构,以及变构蛋白中首选的折叠结构是什么,这些都需要进一步探索。变构位点在多聚体或多结构域蛋白质中更常见于链之间或域之间,而在单体单结构域蛋白质中,它们通常位于变构部位的蛋白质结构的相反侧。虽然大多数折叠结构存在于变构蛋白中,但免疫球蛋白样折叠很少被使用。典型的调节结构域包括α-β 折叠、PDZ 结构域、WW 结构域等。根据对变构调节的理解,已经合理设计了新型变构蛋白和材料。

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