8XI9
Crystal structure of FRB-FKBP fusion protein in complex with rapamycin
Summary for 8XI9
| Entry DOI | 10.2210/pdb8xi9/pdb |
| Descriptor | FRB-FKBP fusion protein, RAPAMYCIN IMMUNOSUPPRESSANT DRUG (3 entities in total) |
| Functional Keywords | rapamycin, signaling protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 1 |
| Total formula weight | 24244.86 |
| Authors | Inobe, T.,Sakaguchi, R.,Obita, T.,Mukaiyama, A.,Yokoyama, T.,Mizuguchi, M.,Akiyama, S. (deposition date: 2023-12-19, release date: 2024-08-07, Last modification date: 2024-10-09) |
| Primary citation | Inobe, T.,Sakaguchi, R.,Obita, T.,Mukaiyama, A.,Koike, S.,Yokoyama, T.,Mizuguchi, M.,Akiyama, S. Structural insights into rapamycin-induced oligomerization of a FRB-FKBP fusion protein. Febs Lett., 598:2292-2305, 2024 Cited by PubMed Abstract: Inducible dimerization systems, such as rapamycin-induced dimerization of FK506 binding protein (FKBP) and FKBP-rapamycin binding (FRB) domain, are widely employed chemical biology tools to manipulate cellular functions. 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. Here, we report that FRB-FKBP forms a rotationally symmetric trimer in crystals, but a larger oligomer in solution, primarily tetramers and pentamers, which maintain similar inter-subunit contacts as in the crystal trimer. These findings expand the applications of the FRB-FKBP oligomerization system in diverse biological events. PubMed: 39031920DOI: 10.1002/1873-3468.14986 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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