6UCL

Transcription factor deltaFosB bZIP domain self-assembly, type-I crystal

6UCL の概要

• エントリーDOI: 10.2210/pdb6ucl/pdb
• 関連するPDBエントリー: 6UCI
• 分子名称: Protein fosB, CHLORIDE ION (3 entities in total)
• 機能のキーワード: activator protein-1, basic leucine zipper, bzip, deltafosb, fos, jun, transcription factor, dna-binding protein, coiled-coil, transcription
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8373.65

構造登録者

Yin, Z.,Machius, M.,Rudenko, G. (登録日: 2019-09-16, 公開日: 2020-01-15, 最終更新日: 2024-11-20)

主引用文献

Yin, Z.,Venkannagari, H.,Lynch, H.,Aglyamova, G.,Bhandari, M.,Machius, M.,Nestler, E.J.,Robison, A.J.,Rudenko, G.
Self-assembly of the bZIP transcription factor Delta FosB.
Curr Res Struct Biol, 2:1-13, 2020

PubMed Abstract: ΔFosB is a highly stable transcription factor that accumulates in specific brain regions upon chronic exposure to drugs of abuse, stress, or seizures, and mediates lasting behavioral responses. ΔFosB reportedly heterodimerizes with JunD forming a canonical bZIP leucine zipper coiled coil that clamps onto DNA. However, the striking accumulation of ΔFosB protein in brain upon chronic insult has brought its molecular status into question. Here, we demonstrate through a series of crystal structures that the ΔFosB bZIP domain self-assembles into stable oligomeric assemblies that defy the canonical arrangement. The ΔFosB bZIP domain also self-assembles in solution, and in neuron-like Neuro 2a cells it is trapped into molecular arrangements that are consistent with our structures. Our data suggest that, as ΔFosB accumulates in brain in response to chronic insult, it forms non-canonical assemblies. These species may be at the root of ΔFosB's striking protein stability, and its unique transcriptional and behavioral consequences.

PubMed: 32542236
DOI: 10.1016/j.crstbi.2019.12.001

実験手法

X-RAY DIFFRACTION (2.207 Å)