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Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4

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 a... Full description

Journal Title: Structure 06 July 2016, Vol.24(7), pp.1201-1208
Main Author: Zhang, Qiang
Other Authors: Zeng, Lei , Shen, Chen , Ju, Ying , Konuma, Tsuyoshi , Zhao, Chengcheng , Vakoc, Christopher r , Zhou, Ming-Ming
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0969-2126 ; E-ISSN: 1878-4186 ; DOI: 10.1016/j.str.2016.04.019
Link: https://www.sciencedirect.com/science/article/pii/S096921261630082X
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recordid: elsevier_sdoi_10_1016_j_str_2016_04_019
title: Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4
format: Article
creator:
  • Zhang, Qiang
  • Zeng, Lei
  • Shen, Chen
  • Ju, Ying
  • Konuma, Tsuyoshi
  • Zhao, Chengcheng
  • Vakoc, Christopher r
  • Zhou, Ming-Ming
subjects:
  • Biology
ispartof: Structure, 06 July 2016, Vol.24(7), pp.1201-1208
description: 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. Zhang et al. report that the ET domain of BRD4 recognizes an amphipathic motif through a two-strand antiparallel β sheet. This structural mechanism explains BRD4 association with cellular and viral proteins including Kaposi's sarcoma-associated herpesvirus LANA, and NSD3 whose interaction with BRD4 via the ET domain is essential for AML maintenance.
language: eng
source:
identifier: ISSN: 0969-2126 ; E-ISSN: 1878-4186 ; DOI: 10.1016/j.str.2016.04.019
fulltext: fulltext
issn:
  • 0969-2126
  • 09692126
  • 1878-4186
  • 18784186
url: Link


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titleStructural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4
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descriptionThe 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. Zhang et al. report that the ET domain of BRD4 recognizes an amphipathic motif through a two-strand antiparallel β sheet. This structural mechanism explains BRD4 association with cellular and viral proteins including Kaposi's sarcoma-associated herpesvirus LANA, and NSD3 whose interaction with BRD4 via the ET domain is essential for AML maintenance.
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titleStructural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4
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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.

Zhang et al. report that the ET domain of BRD4 recognizes an amphipathic motif through a two-strand antiparallel β sheet. This structural mechanism explains BRD4 association with cellular and viral proteins including Kaposi's sarcoma-associated herpesvirus LANA, and NSD3 whose interaction with BRD4 via the ET domain is essential for AML maintenance.

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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.

Zhang et al. report that the ET domain of BRD4 recognizes an amphipathic motif through a two-strand antiparallel β sheet. This structural mechanism explains BRD4 association with cellular and viral proteins including Kaposi's sarcoma-associated herpesvirus LANA, and NSD3 whose interaction with BRD4 via the ET domain is essential for AML maintenance.

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