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人类微小泛素相关修饰蛋白Pin1和Par14/17的结构与功能

Structure and function of the human parvulins Pin1 and Par14/17.

作者信息

Matena Anja, Rehic Edisa, Hönig Dana, Kamba Bianca, Bayer Peter

机构信息

Structural and Medicinal Biochemistry, Center for Medical Biotechnology (ZMB), Faculty of Biology, University of Duisburg-Essen, Universitätsstr. 2, D-45117 Essen, Germany.

出版信息

Biol Chem. 2018 Jan 26;399(2):101-125. doi: 10.1515/hsz-2017-0137.

Abstract

Parvulins belong to the family of peptidyl-prolyl cis/trans isomerases (PPIases) assisting in protein folding and in regulating the function of a broad variety of proteins in all branches of life. The human representatives Pin1 and Par14/17 are directly involved in processes influencing cellular maintenance and cell fate decisions such as cell-cycle progression, metabolic pathways and ribosome biogenesis. This review on human parvulins summarizes the current knowledge of these enzymes and intends to oppose the well-studied Pin1 to its less well-examined homolog human Par14/17 with respect to structure, catalytic and cellular function.

摘要

小脯氨酸异构酶属于肽基脯氨酰顺反异构酶(PPIase)家族,有助于蛋白质折叠,并调节生命各分支中多种蛋白质的功能。人类的代表蛋白Pin1和Par14/17直接参与影响细胞维持和细胞命运决定的过程,如细胞周期进程、代谢途径和核糖体生物发生。这篇关于人类小脯氨酸异构酶的综述总结了这些酶的现有知识,并打算在结构、催化和细胞功能方面,将研究充分的Pin1与其研究较少的同源物人类Par14/17进行对比。

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