Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1

• Main Authors: Xu, X, Li, Y, Bharath, S.R, Ozturk, M.B, Bowler, M.W, Loo, B.Z.L, Tergaonkar, V, Song, H
• Other Authors: BIOCHEMISTRY
• Format: Article
• Published: Nature Publishing Group 2020
• Subjects: DNA fragment; immunoglobulin enhancer binding protein; protein p52; transcription factor Ets 1; disulfide; DNA; ETS1 protein, human; protein binding; telomerase; TERT protein, human; cancer; chemical binding; complexity; crystal structure; inhibition; mutation; reactivation; Article; binding affinity; DNA binding; ETS domain; gene activation; HEK293T cell line; human; human cell; immunoprecipitation; multiple cancer; promoter region; protein protein interaction; signal transduction; TERT gene; transactivation; binding site; chemistry; enzyme activation; Escherichia coli; genetics; HEK293 cell line; metabolism; protein multimerization; X ray crystallography; Binding Sites; Crystallography, X-Ray; Disulfides; Enzyme Activation; HEK293 Cells; Humans; NF-kappa B; NF-kappa B p52 Subunit; Promoter Regions, Genetic; Protein Binding; Protein Multimerization; Proto-Oncogene Protein c-ets-1; Signal Transduction; Telomerase
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/174210
• Institution: National University of Singapore

10.1038/s41467-018-05644-0