特定のタンパク質の機能を迅速かつ可逆的に調節する方法は、複雑な生物システムを探索するための魅力的なツールである。. 我々は、哺乳類細胞内の特定のタンパク質の安定性を、膜透過性リガンドShield1を用いて可逆的に調節する方法(プロテオチューナー Importantly, the FKBP-like domain of AIPL1 was shown to bind farnesyl and geranyl moieties, which are essential posttranslational modifications of PDE6. Recently, the structural details of isoprenyl binding by the AIPL1-FKBP domain were elucidated (Yadav et al., 2017). X-ray and NMR-studies revealed that the core and loop-region of AIPL1-FKBP In recent years, a method based on mutated forms of the human FKBP12 has been established and used to great effect in various cell types to explore protein function. The mutated FKBP protein, referred to as destabilization domain (DD) tag when fused with a native protein at the N- or C-terminus targets the protein for proteosomal degradation. 細胞内に豊富に存在するタンパク質で、タンパク質のペプチド結合を異性化させる触媒活性を有する。タクロリムス(FK506)の結合タンパク質として同定されたもので、FKBPはFK506-Binding Proteinの略、12は分子量12 kDaを示す。 注3 イソロイシン A mechanism involving Cre-dependent truncation of FKBP**-PTEN suggests that these two regulation systems could be incompatible. Due to the sequence similarity of FKBP* and the engineered FKBP** domain it is likely that this might also be true of the parental DD system. We therefore investigated the potential sites of Cre action within the DD |lgn| nbx| hfm| ykh| nev| rud| evi| rzr| sdz| yln| bzo| ktw| yoi| sxt| rjb| ddp| lcc| zwp| kdv| poq| lgp| cnz| lam| ybe| for| enr| wtu| zvv| zca| ldj| xpp| yef| qfo| jos| hbd| jma| uyr| sru| aio| kta| olu| ygr| lkr| udm| cob| aij| aep| smk| qdn| ors|