8yfi

From Proteopedia

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

Structural highlights

8yfi is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.02Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRIP4_HUMAN Transcription coactivator of nuclear receptors which functions in conjunction with CBP-p300 and SRC-1 and may play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a pivotal role in the transactivation of NF-kappa-B, SRF and AP1. Acts as a mediator of transrepression between nuclear receptor and either AP1 or NF-kappa-B. Plays a role in androgen receptor transactivation and in testicular function (By similarity).^[1]

Publication Abstract from PubMed

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.

Biochemical and structural characterization of the DNA-binding properties of human TRIP4 ASCH domain reveals insights into its functional role.,Hu C, Chen Z, Wang G, Yang H, Ding J Structure. 2024 May 30:S0969-2126(24)00189-8. doi: 10.1016/j.str.2024.05.012. PMID:38870938^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jung DJ, Sung HS, Goo YW, Lee HM, Park OK, Jung SY, Lim J, Kim HJ, Lee SK, Kim TS, Lee JW, Lee YC. Novel transcription coactivator complex containing activating signal cointegrator 1. Mol Cell Biol. 2002 Jul;22(14):5203-11. PMID:12077347
↑ 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. 2024 May 30:S0969-2126(24)00189-8. PMID:38870938 doi:10.1016/j.str.2024.05.012