2KHC
Bruno RRM3+
2KHC の概要
エントリーDOI | 10.2210/pdb2khc/pdb |
NMR情報 | BMRB: 16236 |
分子名称 | Testis-specific RNP-type RNA binding protein (1 entity in total) |
機能のキーワード | rrm, rna recognition motif, bruno, rna binding protein |
由来する生物種 | Drosophila melanogaster (Fruit fly) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 12296.02 |
構造登録者 | Lyon, A.M.,Reveal, B.S.,Macdonald, P.M.,Hoffman, D.W. (登録日: 2009-04-01, 公開日: 2009-12-22, 最終更新日: 2024-05-22) |
主引用文献 | Lyon, A.M.,Reveal, B.S.,Macdonald, P.M.,Hoffman, D.W. Bruno protein contains an expanded RNA recognition motif. Biochemistry, 48:12202-12212, 2009 Cited by PubMed Abstract: The RNA recognition motif (or RRM) is a ubiquitous RNA-binding module present in approximately 2% of the proteins encoded in the human genome. This work characterizes an expanded RRM, which is present in the Drosophila Bruno protein, and targets regulatory elements in the oskar mRNA through which Bruno controls translation. In this Bruno RRM, the deletion of 40 amino acids prior to the N-terminus of the canonical RRM resulted in a significantly decreased affinity of the protein for its RNA target. NMR spectroscopy showed that the expanded Bruno RRM contains the familiar RRM fold of four antiparallel beta-strands and two alpha-helices, preceded by a 10-residue loop that contacts helix alpha(1) and strand beta(2); additional amino acids at the N-terminus of the domain are relatively flexible in solution. NMR results also showed that a truncated form of the Bruno RRM, lacking the flexible N-terminal amino acids, forms a stable and complete canonical RRM, so that the loss of RNA binding activity cannot be attributed to disruption of the RRM fold. This expanded Bruno RRM provides a new example of the features that are important for RNA recognition by an RRM-containing protein. PubMed: 19919093DOI: 10.1021/bi900624j 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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