View source for 5emo

==Structure of the star domain of T-STAR in complex with AUUAAA RNA==
<StructureSection load='5emo' size='340' side='right' caption='[[5emo]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5emo]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EMO FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5emo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5emo OCA], [http://pdbe.org/5emo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5emo RCSB], [http://www.ebi.ac.uk/pdbsum/5emo PDBsum]</span></td></tr>
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== Function ==
[[http://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>  
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== 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>
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== References ==
<references/>
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</StructureSection>
[[Category: Dominguez, C]]
[[Category: Feracci, M]]
[[Category: Protein - rna complexes star protein alternative splicing kh domain]]
[[Category: Rna binding protein]]