6GMX
pVHL:EloB:EloC in complex with 6-chlorothiochroman-4-one
Summary for 6GMX
| Entry DOI | 10.2210/pdb6gmx/pdb |
| Descriptor | Elongin-B, Elongin-C, von Hippel-Lindau disease tumor suppressor, ... (9 entities in total) |
| Functional Keywords | e3 ubiquitin ligase, tumor supressor, protac, fragment-based drug discovery, oncoprotein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 12 |
| Total formula weight | 167704.85 |
| Authors | Van Molle, I.,Lucas, X.,Ciulli, A. (deposition date: 2018-05-28, release date: 2018-08-08, Last modification date: 2018-09-05) |
| Primary citation | Lucas, X.,Van Molle, I.,Ciulli, A. Surface Probing by Fragment-Based Screening and Computational Methods Identifies Ligandable Pockets on the von Hippel-Lindau (VHL) E3 Ubiquitin Ligase. J. Med. Chem., 61:7387-7393, 2018 Cited by PubMed Abstract: Beyond the targeting of E3 ubiquitin ligases to inhibit protein homeostasis, E3 ligase binders can be repurposed as targeted protein degraders (PROTACs or molecular glues). We sought to identify new binders of the VHL E3 ligase by biophysical fragment-based screening followed by X-ray crystallographic soaking. We identified fragments binding at the ElonginC:Cullin2 interface and a new cryptic pocket in VHL, along with other potential ligandable sites predicted computationally and found to bind solvent molecules in crystal structures. The elucidated interactions provide starting points for future ligand development. PubMed: 30040896DOI: 10.1021/acs.jmedchem.8b00842 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.533 Å) |
Structure validation
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