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| {{STRUCTURE_3bs9| PDB=3bs9 | SCENE= }} | | {{STRUCTURE_3bs9| PDB=3bs9 | SCENE= }} |
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| '''X-ray structure of human TIA-1 RRM2'''
| | ===X-ray structure of human TIA-1 RRM2=== |
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| ==Overview==
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| 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 1.95A 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18201561}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18201561 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18201561}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rna-binding]] | | [[Category: Rna-binding]] |
| [[Category: Rrm]] | | [[Category: Rrm]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:35:58 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:14:28 2008'' |
