کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1936398 1050690 2008 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Structure of the central RNA recognition motif of human TIA-1 at 1.95 Å resolution
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Structure of the central RNA recognition motif of human TIA-1 at 1.95 Å resolution
چکیده انگلیسی

T-cell-restricted intracellular antigen-1 (TIA-1) regulates alternative pre-mRNA splicing in the nucleus, and mRNA translation in the cytoplasm, by recognizing uridine-rich sequences of RNAs. As a step towards understanding RNA recognition by this regulatory factor, the X-ray structure of the central RNA recognition motif (RRM2) of human TIA-1 is presented at 1.95 Å resolution. Comparison with structurally homologous RRM-RNA complexes identifies residues at the RNA interfaces that are conserved in TIA-1–RRM2. The versatile capability of RNP motifs to interact with either proteins or RNA is reinforced by symmetry-related protein–protein interactions mediated by the RNP motifs of TIA-1–RRM2. Importantly, the TIA-1–RRM2 structure reveals the locations of mutations responsible for inhibiting nuclear import. In contrast with previous assumptions, the mutated residues are buried within the hydrophobic interior of the domain, where they would be likely to destabilize the RRM fold rather than directly inhibit RNA binding.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 367, Issue 4, 21 March 2008, Pages 813–819
نویسندگان
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