FK506-Binding Proteins and Their Diverse Functions.

FK506-Binding Proteins and Their Diverse Functions.
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DOI:
10.2174/1874467208666150519113541
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发表时间:
2015
影响因子:
2.7
通讯作者:
Jiang Y
Jiang Y
中科院分区:
生物学3区
文献类型:
--
作者:
Tong M;Jiang Y

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FK506 结合蛋白 (FKBP) 是真核生物中高度保守的蛋白质家族。该蛋白家族的原型 FKBP12 是免疫抑制药物 FK506 和雷帕霉素的结合伴侣。 FKBP12 作为顺/反肽基脯氨酰异构酶 (PPIase) 发挥作用,催化脯氨酰顺/反构象之间的相互转化。 FKBP 家族成员包含一个或多个 PPIase 结构域,这些结构域并不总是表现出 PPIase 活性,但对于其功能来说都是必需的。 FKBP 参与多种细胞功能,包括蛋白质折叠、细胞信号传导、细胞凋亡和转录。它们通过直接结合和改变靶蛋白的构象来发挥其功能,从而充当分子开关。在这篇综述中,我们对哺乳动物细胞中发现的 FKBP 的结构和多种功能进行了总体总结。
FK506 binding proteins (FKBPs) are a family of highly conserved proteins in eukaryotes. The prototype of this protein family, FKBP12, is the binding partner for immunosuppressive drugs FK506 and rapamycin. FKBP12 functions as a cis/trans peptidyl prolyl isomerase (PPIase) that catalyzes interconversion between prolyl cis/trans conformations. Members of the FKBP family contain one or several PPIase domains, which do not always exhibit PPIase activity yet are all essential for their function. FKBPs are involved in diverse cellular functions including protein folding, cellular signaling, apoptosis and transcription. They elicit their function through direct binding and altering conformation of their target proteins, hence acting as molecular switches. In this review, we provide a general summary for the structures and diverse functions of FKBPs found in mammalian cells.
DOI: 10.1016/0092-8674(94)90214-3
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