基于雷帕霉素与FRB结合的蛋白质间相互作用的相关技术  

Advances in Technology Based on the Combination of Rapamycin and FRB Domain Mediated Protein-protein Interactions

作　　者：李芹芹[1] 史道华[2] 杨牛牛[1] 

机构地区：[1]福建中医药大学药学院,福州350108 [2]南京军区福州总医院药学科,福州350025

出　　处：《生物技术通报》2011年第9期44-47,共4页Biotechnology Bulletin

基　　金：福建省自然基金资助项目(2008J0103)

摘　　要：FKBP12-rapamycin复合物的结合位点(FKBP12-rapamycin binding,FRB)为雷帕霉素(rapamycin,RAP)与哺乳动物雷帕霉素靶蛋白(mammalian target of rapamycin,mTOR)结合的结构域,基于RAP介导FK506结合蛋白12(12 kD FK506-bin-ging protein,FKBP12)与FRB蛋白质相互作用相关研究技术的发展与应用,使人们对小分子介导的蛋白质相互作用有了更多的认识。就研究RAP作用于FRB域及研究FKBP12-RAP-FRB三元复合物形成的相关技术作一综述,为确认新的mTOR抑制剂的作用机制及认识其他蛋白质间相互作用提供参考。FRB domain（FKBP12-rapamycin binding domain）is a binding site of rapamycin（RAP）which targets on mTOR（mammalian target of rapamycin）.As the research technologies has been used and developed based on the RAP mediated the FKBP12-FRB protein interaction,more and more mechanisms were demonstrated in protein-protein interactions induced by small molecules.In this paper,some technologies were reviewed on the study of RAP-FRB binding and FKBP12-RAP-FRB ternary complex formation which intends to recognize the mechanisms of novel mTOR inhibitors and protein-protein interactions.

关 键 词：FRB域 雷帕霉素 蛋白质间相互作用 技术 

分 类 号：R96[医药卫生—药理学]