We previously advanced an inducible dimerization system into an inducible oligomerization system by developing a bivalent fusion protein, FRB–FKBP, which forms large oligomers upon rapamycin addition and can be used to manipulate cells. However, the oligomeric structure of FRB–FKBP remains unclear. ...
Proteins were derived from several different domains: FK506 binding protein (FKBP) (18), FKBP–rapamycin binding (FRB) domain in FRAP (residues 2021–2113) (8), 27th Ig (I27) domain of the giant muscle protein titin (19), and aminopeptidase N (pepN) (20). FRB and FKBP were fused ...
摘要:FKBP12-rapamycin复合物的结合位点(FKBP12-rapamycinbinding,FRB)为雷帕霉素(rapamycin,RAP)与哺乳动 物雷帕霉素靶蛋白(mammaliantargetofrapamycin,mTOR)结合的结构域,基于RAP介导FK506结合蛋白12(12kDFK506-bin- gingprotein,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...
Alternative Name: mTOR (human FKBP12-rapamycin-binding domain)Host: RabbitImmunogen: Recombinant human mTOR (FKBP12-rapamycin-binding (FRB) domain). UniProt ID: P42345 Application: Chromatin Immunoprecipitation Immunocytochemistry Western Blot (1:2’000) Specificity: Recognizes the FRB domain of fusion...
Essential to its various functions is its ability to bind simultaneously to two different proteins, FKBP and mTOR. Despite its widespread use, a thorough analysis of the interactions between FKBP, rapamycin, and the rapamycin-binding domain of mTOR, FRB, is lacking. To probe the affinities ...
Chaurasia, S., Pieraccini, S., De Gonda, R., Conti, S., & Sironi, M. (2013). Molecular insights into the stabilization of pro- tein-protein interactions with small molecule: The FKBP12-rapamycin-FRB case study. Chemical Physics Letters, 587, 68-74. doi:10.1016/j.cplett.2013.09.042...
Two modes of direct small-molecule inhibition of mTOR activity are known: targeting of the kinase active site and a unique mode in which the small molecule rapamycin, in complex with FKBP12 (the 12-kDa FK506 binding protein), binds to the FRB (FKBP12/rapamycin binding) domain of mTOR and...