FKBP52
FKBP52
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DOI：
10.1016/j.biocel.2004.03.013
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发表时间：
2005-01-01
影响因子：
4
通讯作者：
Sánchez, ER
中科院分区：
文献类型：
--
作者：
Davies, TH;Sánchez, ER
大分子量的亲免素FKBP52是免疫抑制药物FK506的已知靶点。FKBP52表现出肽基脯氨酰顺反异构酶（PPI酶）活性，该活性被FK506的结合抑制，FK506与较小但研究更好的亲免蛋白FKBP12具有相同的性质。然而，与FKBP12不同，FKBP52不介导FK506的免疫抑制作用，并且由于其较大的尺寸，含有额外的许多功能结构域。一种这样的结构是一系列的tetratricopeptide repeat（TPR）结构域，其作为普遍存在且丰富的分子伴侣Hsp90的结合位点。作为TPR蛋白的这种性质最好地表征了FKBP 52的已知细胞作用。在这里，我们回顾FKBP 52的结构特征，并将其与这种蛋白质的进化和多样性功能联系起来。虽然FKBP 52最公认的作用是在类固醇受体信号转导的调节，其他不太知名的功能也进行了讨论。(C)2004爱思唯尔有限公司保留所有权利。
The large molecular-weight immunophilin, FKBP52, is a known target of the immunosuppressive drug FK506. FKBP52 exhibits peptidyl-prolyl cis-trans isomerase (PPIase) activity, which is inhibited by the binding of FK506-properties that it shares with the smaller but better-studied immunophilin, FKBP12. Unlike FKBP12, however, FKBP52 does not mediate the immunosuppressive actions of FK506 and, due to its larger size, contains additional numerous functional domains. One such structure is a series of tetratricopeptide repeat (TPR) domains, which serve as binding sites for the ubiquitous and abundant molecular chaperone, Hsp90. It is this property as a TPR protein that best characterizes the known cellular roles of FKBP52. Here, we review the structural features of FKBP52 and relate them to the evolving and diverse functions of this protein. Although the most recognized role of FKBP52 is in regulation of steroid receptor signaling, other less well-known functions are also discussed. (C) 2004 Elsevier Ltd. All rights reserved.