6RCY
CRYSTAL STRUCTURE OF FK1 DOMAIN OF FKBP52 IN COMPLEX WITH A BIO-INSPIRED HYBRID FLUORESCENT LIGAND
Summary for 6RCY
| Entry DOI | 10.2210/pdb6rcy/pdb |
| Descriptor | Peptidyl-prolyl cis-trans isomerase FKBP4, (2~{S})-5-carbamimidamido-2-[[(2~{S})-2-[[(2~{S})-1-[5-(dimethylamino)naphthalen-1-yl]sulfonylpiperidin-2-yl]carbonylamino]-4-phenyl-butanoyl]amino]pentanoic acid (3 entities in total) |
| Functional Keywords | fkbp52, the n-terminal domain, isomerase, ligand, fluorescence |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 16905.18 |
| Authors | Li de la Sierra-Gallay, I.,Byrne, C. (deposition date: 2019-04-12, release date: 2020-05-13, Last modification date: 2024-01-24) |
| Primary citation | de la Sierra-Gallay, I.L.,Belnou, M.,Chambraud, B.,Genet, M.,van Tilbeurgh, H.,Aumont-Nicaise, M.,Desmadril, M.,Baulieu, E.E.,Jacquot, Y.,Byrne, C. Bioinspired Hybrid Fluorescent Ligands for the FK1 Domain of FKBP52. J.Med.Chem., 63:10330-10338, 2020 Cited by PubMed Abstract: The protein FKBP52 is a steroid hormone receptor coactivator likely involved in neurodegenerative disease. A series of small, water-soluble, bioinspired, pseudopeptidic fluorescent ligands for the FK1 domain of this protein are described. The design is such that engulfing of the ligand in the pocket of this domain is accompanied by hydrogen-bonding of the dansyl chromophore which functions as both an integral part of the ligand and a fluorescent reporter. Binding is concomitant with a significant wavelength shift and an enhancement of the ligand fluorescence signal. Excitation of FK1 domain native tryptophan residues in the presence of bound ligand results in Förster resonance energy transfer. Variation of key ligand residues within the short sequence was undertaken, and the interaction of the resulting library with the protein was measured by techniques including isothermal calorimetry analysis, fluorescence, and FRET quenching, and a range of values were determined. Cocrystallization of a protein ligand complex at 2.30 Å resolution provided detailed information at the atomic scale, while also providing insight into native substrate binding. PubMed: 32866001DOI: 10.1021/acs.jmedchem.0c00825 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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