2NCZ

Solution NMR structures of BRD4 ET domain in complex with NSD3_1 peptide

Summary for 2NCZ

• Entry DOI: 10.2210/pdb2ncz/pdb
• Related: 2ND0 2ND1
• NMR Information: BMRB: 26041
• Descriptor: Bromodomain-containing protein 4, Histone-lysine N-methyltransferase NSD3 (2 entities in total)
• Functional Keywords: transcription, transferase, transcription-transferase complex, transcription/transferase
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: O60885 Q9BZ95
• Total number of polymer chains: 2
• Total formula weight: 11176.88

Authors

Zeng, L.,Zhou, M. (deposition date: 2016-04-18, release date: 2016-06-29, Last modification date: 2024-05-01)

Primary citation

Zhang, Q.,Zeng, L.,Shen, C.,Ju, Y.,Konuma, T.,Zhao, C.,Vakoc, C.R.,Zhou, M.M.
Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4.
Structure, 24:1201-1208, 2016

PubMed Abstract: The bromodomains and extra-terminal domain (BET) proteins direct gene transcription in chromatin, and represent new drug targets for cancer and inflammation. Here we report that the ET domain of the BET protein BRD4 recognizes an amphipathic protein sequence motif through establishing a two-strand antiparallel β sheet anchored on a hydrophobic cleft of the three-helix bundle. This structural mechanism likely explains BRD4 interactions with numerous cellular and viral proteins such as Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen, and NSD3 whose interaction with BRD4 via this ET domain mechanism is essential for acute myeloid leukemia maintenance.

PubMed: 27291650
DOI: 10.1016/j.str.2016.04.019

Experimental method

SOLUTION NMR