6JEY
Covalent bond formation between ynone moiety of synthetic fatty acid and hPPARg-LBD
Summary for 6JEY
| Entry DOI | 10.2210/pdb6jey/pdb |
| Descriptor | Peroxisome proliferator-activated receptor gamma, (9Z,12Z,15Z,18Z,21Z)-5-oxidanylidenetetracosa-9,12,15,18,21-pentaen-6-ynoic acid (3 entities in total) |
| Functional Keywords | receptor, covalent ligand, ynone, oxo-fatty acid, nuclear protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 64004.57 |
| Authors | Kojima, H.,Yamamoto, K.,Itoh, T. (deposition date: 2019-02-07, release date: 2020-02-12, Last modification date: 2023-11-22) |
| Primary citation | Kojima, H.,Fujita, Y.,Takeuchi, R.,Ikebe, Y.,Ohashi, N.,Yamamoto, K.,Itoh, T. Cyclization Reaction-Based Turn-on Probe for Covalent Labeling of Target Proteins. Cell Chem Biol, 27:334-, 2020 Cited by PubMed Abstract: Fluorescent molecules have contributed to basic biological research but there are currently only a limited number of probes available for the detection of non-enzymatic proteins. Here, we report turn-on fluorescent probes mediated by conjugate addition and cyclization (TCC probes). These probes react with multiple amino acids and exhibit a 36-fold greater emission intensity after reaction. We analyzed the reactions between TCC probes and nuclear receptors by electrospray ionization mass spectrometry, X-ray crystallography, spectrofluorometry, and fluorescence microscopy. In vitro analysis showed that probes consisting of a protein ligand and TCC could label vitamin D receptor and peroxisome proliferator-activated receptor γ. Moreover, we demonstrated that not only a ligand unit but also a peptide unit can label the target protein in a complex mixture. PubMed: 31991094DOI: 10.1016/j.chembiol.2020.01.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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