Summary for 7QXT
| Entry DOI | 10.2210/pdb7qxt/pdb |
| Descriptor | ATPase family AAA domain-containing protein 2, SULFATE ION, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | atad2, inhibitor, fragment, bromodomain, fraglite, transcription |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 16017.27 |
| Authors | Turberville, S.,Martin, M.P.,Hope, I.,Noble, M.E.M. (deposition date: 2022-01-27, release date: 2022-11-23, Last modification date: 2024-01-31) |
| Primary citation | Davison, G.,Martin, M.P.,Turberville, S.,Dormen, S.,Heath, R.,Heptinstall, A.B.,Lawson, M.,Miller, D.C.,Ng, Y.M.,Sanderson, J.N.,Hope, I.,Wood, D.J.,Cano, C.,Endicott, J.A.,Hardcastle, I.R.,Noble, M.E.M.,Waring, M.J. Mapping Ligand Interactions of Bromodomains BRD4 and ATAD2 with FragLites and PepLites─Halogenated Probes of Druglike and Peptide-like Molecular Interactions. J.Med.Chem., 65:15416-15432, 2022 Cited by PubMed Abstract: The development of ligands for biological targets is critically dependent on the identification of sites on proteins that bind molecules with high affinity. A set of compounds, called FragLites, can identify such sites, along with the interactions required to gain affinity, by X-ray crystallography. We demonstrate the utility of FragLites in mapping the binding sites of bromodomain proteins BRD4 and ATAD2 and demonstrate that FragLite mapping is comparable to a full fragment screen in identifying ligand binding sites and key interactions. We extend the FragLite set with analogous compounds derived from amino acids (termed PepLites) that mimic the interactions of peptides. The output of the FragLite maps is shown to enable the development of ligands with leadlike potency. This work establishes the use of FragLite and PepLite screening at an early stage in ligand discovery allowing the rapid assessment of tractability of protein targets and informing downstream hit-finding. PubMed: 36367089DOI: 10.1021/acs.jmedchem.2c01357 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.51 Å) |
Structure validation
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