| Literature DB >> 27291650 |
Qiang Zhang1, Lei Zeng1, Chen Shen2, Ying Ju3, Tsuyoshi Konuma4, Chengcheng Zhao3, Christopher R Vakoc5, Ming-Ming Zhou6.
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.Entities:
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Year: 2016 PMID: 27291650 PMCID: PMC4938737 DOI: 10.1016/j.str.2016.04.019
Source DB: PubMed Journal: Structure ISSN: 0969-2126 Impact factor: 5.006