8DC8

Crystal structure of p53 Y220C covalently bound to azaindole KG13

Summary for 8DC8

Entry DOI	10.2210/pdb8dc8/pdb
Descriptor	Cellular tumor antigen p53, 2-methyl-1-[(4P)-3-methyl-4-(2-methyl-1,2,3,4-tetrahydroisoquinolin-6-yl)-1H-pyrrolo[2,3-c]pyridin-1-yl]prop-2-en-1-one, bound form, SULFATE ION, ... (6 entities in total)
Functional Keywords	tp53, tumor suppressor, cell cycle
Biological source	Homo sapiens (human)
Total number of polymer chains	1
Total formula weight	25383.16
Authors	Guiley, K.Z.,Shokat, K.M. (deposition date: 2022-06-15, release date: 2022-10-12, Last modification date: 2024-11-06)
Primary citation	Guiley, K.Z.,Shokat, K.M. A Small Molecule Reacts with the p53 Somatic Mutant Y220C to Rescue Wild-type Thermal Stability. Cancer Discov, 13:56-69, 2023 Cited by PubMed Abstract: The transcription factor and tumor suppressor protein p53 is the most frequently mutated and inactivated gene in cancer. Mutations in p53 result in deregulated cell proliferation and genomic instability, both hallmarks of cancer. There are currently no therapies available that directly target mutant p53 to rescue wild-type function. In this study, we identify covalent compsounds that selectively react with the p53 somatic mutant cysteine Y220C and restore wild-type thermal stability. PubMed: 36197521 DOI: 10.1158/2159-8290.CD-22-0381 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.72009735908 Å)

Structure validation