6XAT

Crystal structure of the human FoxP4 DNA binding Domain

6XAT の概要

• エントリーDOI: 10.2210/pdb6xat/pdb
• 分子名称: FOXP4 protein, SODIUM ION (3 entities in total)
• 機能のキーワード: forkhead domain transcription factor, 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: 13235.05

構造登録者

VIllalobos, P.,Castro-Fernandez, V.,Medina, E.,Gonzalez-Ordenes, F.,Maturana, P.,Herrera-Morande, A.,Ramirez-Sarmiento, C.A.,Babul, J. (登録日: 2020-06-04, 公開日: 2021-06-09, 最終更新日: 2024-01-31)

主引用文献

Villalobos, P.,Carvajal, A.I.,Castro-Fernandez, V.,Babul, J.,Ramirez-Sarmiento, C.A.,Medina, E.
Unraveling the folding and dimerization properties of the human FoxP subfamily of transcription factors.
Febs Lett., 597:1894-1905, 2023

PubMed Abstract: Human FoxP proteins share a highly conserved DNA-binding domain that dimerizes via three-dimensional domain swapping, although showing varying oligomerization propensities among its members. Here, we present an experimental and computational characterization of all human FoxP proteins to unravel how their amino acid substitutions impact their folding and dimerization mechanism. We solved the crystal structure of the forkhead domain of FoxP4 to then perform a comparison across all members, finding that their sequence changes impact not only the structural heterogeneity of their forkhead domains but also the protein-protein association energy barrier. Lastly, we demonstrate that the accumulation of a monomeric intermediate is an oligomerization-dependent feature rather than a common aspect of monomers and dimers in this protein subfamily.

PubMed: 37199668
DOI: 10.1002/1873-3468.14665

実験手法

X-RAY DIFFRACTION (2.2 Å)