Diversified targets of FKBP25 and its complex with rapamycin
Diversified targets of FKBP25 and its complex with rapamycin
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DOI：
10.1016/j.ijbiomac.2014.05.060
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发表时间：
2014-08-01
影响因子：
8.2
通讯作者：
Stura, Enrico A.
中科院分区：
文献类型：
--
作者：
Galat, Andrzej;Thai, Robert;Stura, Enrico A.
FKBP25是肽基脯氨酸顺/反式异构酶超家族的成员，是免疫抑制抗生素雷帕霉素（Rpm）的高亲和力结合物。从天然来源分离的FKBP25，其重组小鼠同源物（mFKBP25）及其与雷帕霉素的复合物可结合多种dna、rna和肝素亲和珠。重组mFKBP25/雷帕霉素复合物结合多种蛋白质，包括钙调蛋白- a /钙调蛋白- b /钙调蛋白复合物和延伸因子1 β。我们解决了mFKBP25与雷帕霉素结合的c端结构域的x射线结构，其分辨率高于人类的对应结构，并清楚地表明带正电的40s环是fk506样结合域（FK506-like binding domain， FKBD）与各种生物聚合物相互作用的表位。(C) 2014 Elsevier B.V.版权所有
FKBP25 is a member of the super-family of peptidylprolyl cis/trans isomerases, which is a high affinity binder for the immunosuppressive antibiotic rapamycin (Rpm). FKBP25 isolated from natural sources, its recombinant murine homologue (mFKBP25) and their complexes with rapamycin bind to diverse DNAs, RNAs and heparin affinity beads. The recombinant mFKBP25/rapamycin complex binds to several proteins including the calcineurin-A/calcineurin-B/calmodulin complex and to elongation factor 1 beta. We solved the X-ray structure of the C-terminal domain of mFKBP25 bound to rapamycin that has a higher resolution than of its human counterpart, and which clearly illustrates that the positively charged 40s loop is an epitope of the FK506-like binding domain (FKBD) for interactions with various biopolymers. (C) 2014 Elsevier B.V. All rights reserved.