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6G0S

Crystal Structure of the first bromodomain of human BRD4 in complex with an acetylated SIRT7 peptide (K272ac/K275ac)

Summary for 6G0S
Entry DOI10.2210/pdb6g0s/pdb
DescriptorBromodomain-containing protein 4, NAD-dependent protein deacetylase sirtuin-7, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordsbromodomain, transcription, complex
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains3
Total formula weight31795.64
Authors
Filippakopoulos, P.,Picaud, S.,Krojer, T.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.M.,Bountra, C. (deposition date: 2018-03-19, release date: 2018-11-28, Last modification date: 2024-11-06)
Primary citationLambert, J.P.,Picaud, S.,Fujisawa, T.,Hou, H.,Savitsky, P.,Uuskula-Reimand, L.,Gupta, G.D.,Abdouni, H.,Lin, Z.Y.,Tucholska, M.,Knight, J.D.R.,Gonzalez-Badillo, B.,St-Denis, N.,Newman, J.A.,Stucki, M.,Pelletier, L.,Bandeira, N.,Wilson, M.D.,Filippakopoulos, P.,Gingras, A.C.
Interactome Rewiring Following Pharmacological Targeting of BET Bromodomains.
Mol. Cell, 73:621-638.e17, 2019
Cited by
PubMed Abstract: Targeting bromodomains (BRDs) of the bromo-and-extra-terminal (BET) family offers opportunities for therapeutic intervention in cancer and other diseases. Here, we profile the interactomes of BRD2, BRD3, BRD4, and BRDT following treatment with the pan-BET BRD inhibitor JQ1, revealing broad rewiring of the interaction landscape, with three distinct classes of behavior for the 603 unique interactors identified. A group of proteins associate in a JQ1-sensitive manner with BET BRDs through canonical and new binding modes, while two classes of extra-terminal (ET)-domain binding motifs mediate acetylation-independent interactions. Last, we identify an unexpected increase in several interactions following JQ1 treatment that define negative functions for BRD3 in the regulation of rRNA synthesis and potentially RNAPII-dependent gene expression that result in decreased cell proliferation. Together, our data highlight the contributions of BET protein modules to their interactomes allowing for a better understanding of pharmacological rewiring in response to JQ1.
PubMed: 30554943
DOI: 10.1016/j.molcel.2018.11.006
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.48 Å)
Structure validation

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