3JTG

Crystal structure of mouse Elf3 C-terminal DNA-binding domain in complex with type II TGF-beta receptor promoter DNA

3JTG の概要

• エントリーDOI: 10.2210/pdb3jtg/pdb
• 分子名称: ETS-related transcription factor Elf-3, DNA (5'-D(*GP*AP*GP*GP*AP*GP*TP*TP*TP*CP*CP*TP*GP*TP*TP*T)-3'), DNA (5'-D(*CP*AP*AP*AP*CP*AP*GP*GP*AP*AP*AP*CP*TP*CP*CP*T)-3'), ... (4 entities in total)
• 機能のキーワード: elf3, protein-dna complex, type ii tgf-beta receptor, activator, alternative splicing, cytoplasm, developmental protein, differentiation, dna-binding, inflammatory response, nucleus, repressor, transcription, transcription regulation
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q3UPW2
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 22267.64

構造登録者

Tahirov, T.H.,Babayeva, N.D.,Agarkar, V.B.,Rizzino, A. (登録日: 2009-09-11, 公開日: 2010-01-12, 最終更新日: 2024-02-21)

主引用文献

Agarkar, V.B.,Babayeva, N.D.,Wilder, P.J.,Rizzino, A.,Tahirov, T.H.
Crystal structure of mouse Elf3 C-terminal DNA-binding domain in complex with type II TGF-beta receptor promoter DNA.
J.Mol.Biol., 397:278-289, 2010

PubMed Abstract: The Ets family of transcription factors is composed of more than 30 members. One of its members, Elf3, is expressed in virtually all epithelial cells as well as in many tumors, including breast tumors. Several studies observed that the promoter of the type II TGF-beta receptor gene (TbetaR-II) is strongly stimulated by Elf3 via two adjacent Elf3 binding sites, the A-site and the B-site. Here, we report the 2.2 A resolution crystal structure of a mouse Elf3 C-terminal fragment, containing the DNA-binding Ets domain, in complex with the B-site of mouse type II TGF-beta receptor promoter DNA (mTbetaR-II(DNA)). Elf3 contacts the core GGAA motif of the B-site from a major groove similar to that of known Ets proteins. However, unlike other Ets proteins, Elf3 also contacts sequences of the A-site from the minor groove of the DNA. DNA binding experiments and cell-based transcription studies indicate that minor groove interaction by Arg349 located in the Ets domain is important for Elf3 function. Equally interesting, previous studies have shown that the C-terminal region of Elf3, which flanks the Ets domain, is required for Elf3 binding to DNA. In this study, we determined that Elf3 amino acid residues within this flanking region, including Trp361, are important for the structural integrity of the protein as well as for the Efl3 DNA binding and transactivation activity.

PubMed: 20079749
DOI: 10.1016/j.jmb.2010.01.017

実験手法

X-RAY DIFFRACTION (2.2 Å)