2ND1

Solution NMR structures of BRD4 ET domain in complex with NSD3_3 peptide

2ND1 の概要

• エントリーDOI: 10.2210/pdb2nd1/pdb
• NMR情報: BMRB: 26043
• 分子名称: Bromodomain-containing protein 4, Histone-lysine N-methyltransferase NSD3 (2 entities in total)
• 機能のキーワード: transcription, transferase, transcription-transferase complex, transcription/transferase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: O60885 Q9BZ95
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 11303.07

構造登録者

Zeng, L.,Zhou, M. (登録日: 2016-04-19, 公開日: 2016-06-29, 最終更新日: 2024-05-01)

主引用文献

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

実験手法

SOLUTION NMR