5EV1
Structure I of Intact U2AF65 Recognizing a 3' Splice Site Signal
5EV1 の概要
エントリーDOI | 10.2210/pdb5ev1/pdb |
関連するPDBエントリー | 5EV2 5EV3 5EV4 |
分子名称 | Splicing factor U2AF 65 kDa subunit, DNA/RNA (5'-R(*UP*UP*U)-D(P*UP*UP*(BRU)P*U)-R(P*UP*U)-3'), SODIUM ION, ... (6 entities in total) |
機能のキーワード | protein-rna complex, rna splicing factor, rna recognition motif, polypyrimidine tract, rna binding protein-rna complex, rna binding protein/rna |
由来する生物種 | Homo sapiens (Human) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 24997.71 |
構造登録者 | |
主引用文献 | Agrawal, A.A.,Salsi, E.,Chatrikhi, R.,Henderson, S.,Jenkins, J.L.,Green, M.R.,Ermolenko, D.N.,Kielkopf, C.L. An extended U2AF(65)-RNA-binding domain recognizes the 3' splice site signal. Nat Commun, 7:10950-10950, 2016 Cited by PubMed Abstract: How the essential pre-mRNA splicing factor U2AF(65) recognizes the polypyrimidine (Py) signals of the major class of 3' splice sites in human gene transcripts remains incompletely understood. We determined four structures of an extended U2AF(65)-RNA-binding domain bound to Py-tract oligonucleotides at resolutions between 2.0 and 1.5 Å. These structures together with RNA binding and splicing assays reveal unforeseen roles for U2AF(65) inter-domain residues in recognizing a contiguous, nine-nucleotide Py tract. The U2AF(65) linker residues between the dual RNA recognition motifs (RRMs) recognize the central nucleotide, whereas the N- and C-terminal RRM extensions recognize the 3' terminus and third nucleotide. Single-molecule FRET experiments suggest that conformational selection and induced fit of the U2AF(65) RRMs are complementary mechanisms for Py-tract association. Altogether, these results advance the mechanistic understanding of molecular recognition for a major class of splice site signals. PubMed: 26952537DOI: 10.1038/ncomms10950 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.037 Å) |
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