6XAT

Crystal structure of the human FoxP4 DNA binding Domain

Summary for 6XAT

• Entry DOI: 10.2210/pdb6xat/pdb
• Descriptor: FOXP4 protein, SODIUM ION (3 entities in total)
• Functional Keywords: forkhead domain transcription factor, transcription
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 13235.05

Authors

VIllalobos, P.,Castro-Fernandez, V.,Medina, E.,Gonzalez-Ordenes, F.,Maturana, P.,Herrera-Morande, A.,Ramirez-Sarmiento, C.A.,Babul, J. (deposition date: 2020-06-04, release date: 2021-06-09, Last modification date: 2024-01-31)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)