View source for 8yfi


==TRIP4 ASCH domain in complex with a 12bp dsDNA (5'-TGAGGTACCTCA-3')==
<StructureSection load='8yfi' size='340' side='right'caption='[[8yfi]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8yfi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8YFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YFI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8yfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8yfi OCA], [https://pdbe.org/8yfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8yfi RCSB], [https://www.ebi.ac.uk/pdbsum/8yfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8yfi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRIP4_HUMAN 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).<ref>PMID:12077347</ref> 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:38870938</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8yfi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ding J]]
[[Category: Hu C]]
[[Category: Yang H]]