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Backbone assignment of the UHM domain of Puf60 free and bound to five ligands |
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| Authors: | Lorenzo Corsini Michael Sattler |
| Institution: | 1. Structural and Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstr. 1, Heidelberg, D-69117, Germany 2. Institute of Structural Biology, Helmholtz Zentrum München, Ingolst?dter Landstr. 1, 85764, Neuherberg, Germany 3. Department Chemie, Munich Center for Integrated Protein Science and Chair Biomolecular NMR, Technische Universit?t München, Lichtenbergstr. 4, 85747, Garching, Germany |
| Abstract: | U2AF homology motifs (UHM) are protein domains that bind peptidic UHM ligand motifs (ULM) and thus form an intricate network of interactions involved in splicing regulation. Here, we report the backbone assignment of the UHM domain of the splicing factor Puf60 as well as 1H, 15N chemical shifts upon binding of the ULM peptides U2AF65 (85–112), SF1 (1–25), SF3b155 (194–229), SF3b155 (317–357), and Prp16 (201–238). |
| Keywords: | Splicing Alternative splicing FBP interacting repressor UHM ULM Chemical shift perturbation |
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