2WTY

Crystal structure of the homodimeric MafB in complex with the T-MARE binding site

2WTY の概要

• エントリーDOI: 10.2210/pdb2wty/pdb
• 関連するPDBエントリー: 2WT7
• 分子名称: TRANSCRIPTION FACTOR MAFB, DNA (5'-D(*TP*AP*AP*TP*TP*GP*CP*TP*GP*AP*CP*TP*CP*AP *GP*CP*AP*AP*AP*T)-3'), DNA (5'-D(*TP*AP*TP*TP*TP*GP*CP*TP*GP*AP*GP*TP*CP*AP *GP*CP*AP*AP*TP*T)-3'), ... (5 entities in total)
• 機能のキーワード: repressor, dna-binding, transcription, proto-oncogene, transcription regulation, tumor suppressor, dna, b-zip, nucleus, activator, ap-1 binding site, protein-dna complex
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE)
• 細胞内の位置: Nucleus: P54841
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 35675.18

構造登録者

Consani Textor, L.,Holton, S.,Wilmanns, M. (登録日: 2009-09-25, 公開日: 2010-12-08, 最終更新日: 2024-05-08)

主引用文献

Pogenberg, V.,Consani Textor, L.,Vanhille, L.,Holton, S.J.,Sieweke, M.H.,Wilmanns, M.
Design of a bZIP Transcription Factor with Homo/Heterodimer-Induced DNA-Binding Preference.
Structure, 22:466-, 2014

PubMed Abstract: The ability of basic leucine zipper transcription factors for homo- or heterodimerization provides a paradigm for combinatorial control of eukaryotic gene expression. It has been unclear, however, how facultative dimerization results in alternative DNA-binding repertoires on distinct regulatory elements. To unravel the molecular basis of such coupled preferences, we determined two high-resolution structures of the transcription factor MafB as a homodimer and as a heterodimer with c-Fos bound to variants of the Maf-recognition element. The structures revealed several unexpected and dimer-specific coiled-coil-heptad interactions. Based on these findings, we have engineered two MafB mutants with opposite dimerization preferences. One of them showed a strong preference for MafB/c-Fos heterodimerization and enabled selection of heterodimer-favoring over homodimer-specific Maf-recognition element variants. Our data provide a concept for transcription factor design to selectively activate dimer-specific pathways and binding repertoires.

PubMed: 24530283
DOI: 10.1016/J.STR.2013.12.017

実験手法

X-RAY DIFFRACTION (2.9 Å)