ASSOCIATION OF A 59-KILODALTON IMMUNOPHILIN WITH THE GLUCOCORTICOID RECEPTOR COMPLEX
ASSOCIATION OF A 59-KILODALTON IMMUNOPHILIN WITH THE GLUCOCORTICOID RECEPTOR COMPLEX
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DOI：
10.1126/science.1376003
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发表时间：
1992-05-29
期刊：
影响因子：
56.9
通讯作者：
SCHREIBER, SL
中科院分区：
文献类型：
--
作者：
TAI, PKK;ALBERS, MW;SCHREIBER, SL
亲免素是一类在体外表现出旋转异构酶（肽基脯氨酰顺反异构酶）活性的蛋白质家族，在许多生物体中表达，并且大多数亲免素可以介导FK506、雷帕霉素和环孢菌素A的免疫抑制作用，未连接蛋白的生理作用尚不清楚。一个59千道尔顿的FK506和雷帕霉素结合类的成员被发现在没有这些药物的情况下与两个热休克蛋白（hsp90和hsp70）和糖皮质激素受体（GR）。这些蛋白质共同组成了无活性的GR，从而在生物化学上连接了两个蛋白质家族，这两个蛋白质家族被认为参与蛋白质折叠组装以及两种有效的免疫抑制方式。
Immunophilins, a family of proteins that exhibit rotamase (peptidyl-prolyl cis-trans isomerase) activity in vitro, are expressed in many organisms and most some immunophilins can mediate the immunosuppressive actions of FK506, rapamycin, and cyclosporin A, the physiological role of the unligated proteins is not known. A 59-kilodalton member of the FK506- and rapamycin-binding class was found to associate in the absence of these drugs with two heat shock proteins (hsp90 and hsp70) and the glucocorticoid receptor (GR). Together, these proteins make up the inactive GR, thus biochemically linking two families of proteins proposed to be involved in protein folding assembly as well as two potent immunosuppressive modalities.