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5ELS

Structure of the KH domain of T-STAR in complex with AAAUAA RNA

Summary for 5ELS
Entry DOI10.2210/pdb5els/pdb
DescriptorKH domain-containing, RNA-binding, signal transduction-associated protein 3, RNA (5'-R(P*AP*AP*AP*UP*AP*A)-3'), SULFATE ION (3 entities in total)
Functional Keywordsprotein - rna complexes star protein alternative splicing kh domain, rna binding protein
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus : O75525
Total number of polymer chains8
Total formula weight81191.06
Authors
Dominguez, C.,Feracci, M. (deposition date: 2015-11-05, release date: 2016-01-13, Last modification date: 2024-05-08)
Primary citationFeracci, M.,Foot, J.N.,Grellscheid, S.N.,Danilenko, M.,Stehle, R.,Gonchar, O.,Kang, H.S.,Dalgliesh, C.,Meyer, N.H.,Liu, Y.,Lahat, A.,Sattler, M.,Eperon, I.C.,Elliott, D.J.,Dominguez, C.
Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68.
Nat Commun, 7:10355-10355, 2016
Cited by
PubMed Abstract: 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.
PubMed: 26758068
DOI: 10.1038/ncomms10355
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.873 Å)
Structure validation

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