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. ...
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...
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 ...
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...
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...
•Fusion proteins containing FRB and FKBP formed oligomers on adding rapamycin.•Various oligomers were generated by adjusting the configuration of fusion proteins.•FRB–FKBP fusion protein without a linker (FR–FK) specifically formed a tetramer.•Proteins fused to FR–FK also formed a tetram...
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 a...
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. Molecular insights into the stabilization of protein-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 (2013)....
The structure of the FKBP12–rapamycin–FRB ternary complex has now been refined at 2.2 Å resolution. The cell-cycle arrest agent rapamycin binds FK506-binding protein (FKBP12) and the FKBP12–rapamycin binding (FRB) domain of FKBP12–rapamycin associated protein (FRAP) simultaneously, and...