View source for 5elt


==Structure of the QUA1-KH domain of T-STAR in complex with UAAU RNA==
<StructureSection load='5elt' size='340' side='right'caption='[[5elt]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5elt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ELT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ELT 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]] 2.13&#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=5elt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5elt OCA], [https://pdbe.org/5elt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5elt RCSB], [https://www.ebi.ac.uk/pdbsum/5elt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5elt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KHDR3_HUMAN KHDR3_HUMAN] RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. May play a role as a negative regulator of cell growth. Inhibits cell proliferation. Involved in splice site selection of vascular endothelial growth factor. Induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer. RNA-binding abilities are down-regulated by tyrosine kinase PTK6. Involved in post-transcriptional regulation of HIV-1 gene expression. Binds preferentially to the 5'-[AU]UAAA-3' motif in vitro.<ref>PMID:10564820</ref> <ref>PMID:11741900</ref> <ref>PMID:15901763</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sam68 and T-STAR are members of the STAR family of proteins that directly link signal transduction with post-transcriptional gene regulation. Sam68 controls the alternative splicing of many oncogenic proteins. T-STAR is a tissue-specific paralogue that regulates the alternative splicing of neuronal pre-mRNAs. STAR proteins differ from most splicing factors, in that they contain a single RNA-binding domain. Their specificity of RNA recognition is thought to arise from their property to homodimerize, but how dimerization influences their function remains unknown. Here, we establish at atomic resolution how T-STAR and Sam68 bind to RNA, revealing an unexpected mode of dimerization different from other members of the STAR family. We further demonstrate that this unique dimerization interface is crucial for their biological activity in splicing regulation, and suggest that the increased RNA affinity through dimer formation is a crucial parameter enabling these proteins to select their functional targets within the transcriptome.

Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68.,Feracci M, Foot JN, Grellscheid SN, Danilenko M, Stehle R, Gonchar O, Kang HS, Dalgliesh C, Meyer NH, Liu Y, Lahat A, Sattler M, Eperon IC, Elliott DJ, Dominguez C Nat Commun. 2016 Jan 13;7:10355. doi: 10.1038/ncomms10355. PMID:26758068<ref>PMID:26758068</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5elt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Dominguez C]]
[[Category: Feracci M]]