8YFI

TRIP4 ASCH domain in complex with a 12bp dsDNA (5'-TGAGGTACCTCA-3')

Summary for 8YFI

• Entry DOI: 10.2210/pdb8yfi/pdb
• Descriptor: Activating signal cointegrator 1, DNA (5'-D(*TP*GP*AP*GP*GP*TP*AP*CP*CP*TP*CP*A)-3') (3 entities in total)
• Functional Keywords: asch domain, complex, dna binding protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 20586.07

Authors

Ding, J.,Yang, H.,Hu, C. (deposition date: 2024-02-24, release date: 2024-06-26, Last modification date: 2024-08-28)

Primary citation

Hu, C.,Chen, Z.,Wang, G.,Yang, H.,Ding, J.
Biochemical and structural characterization of the DNA-binding properties of human TRIP4 ASCH domain reveals insights into its functional role.
Structure, 32:1208-, 2024

PubMed Abstract: TRIP4 is a conserved transcriptional coactivator that is involved in the regulation of the expression of multiple genes. It consists of a classical N-terminal C2HC5-like zinc-finger domain and a conserved C-terminal ASCH domain. Here, we characterized the DNA-binding properties of the human TRIP4 ASCH domain. Our biochemical data show that TRIP4-ASCH has comparable binding affinities toward ssDNA and dsDNA of different lengths, sequences, and structures. The crystal structures reveal that TRIP4-ASCH binds to DNA substrates in a sequence-independent manner through two adjacent positively charged surface patches: one binds to the 5'-end of DNA, and the other binds to the 3'-end of DNA. Further mutagenesis experiments and binding assays confirm the functional roles of key residues involved in DNA binding. In summary, our data demonstrate that TRIP4-ASCH binds to the 5' and 3'-ends of DNA in a sequence-independent manner, which will facilitate further studies of the biological function of TRIP4.

PubMed: 38870938
DOI: 10.1016/j.str.2024.05.012

Experimental method

X-RAY DIFFRACTION (2.02 Å)