3BS9

X-ray structure of human TIA-1 RRM2

Summary for 3BS9

• Entry DOI: 10.2210/pdb3bs9/pdb
• Descriptor: Nucleolysin TIA-1 isoform p40, IODIDE ION (3 entities in total)
• Functional Keywords: rna recognition motif, rrm, rna binding domain, rbd, rna splicing, apoptosis, phosphoprotein, rna-binding, rna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasmic granule: P31483
• Total number of polymer chains: 2
• Total formula weight: 19795.72

Authors

Kumar, A.O.,Kielkopf, C.L. (deposition date: 2007-12-22, release date: 2008-01-15, Last modification date: 2023-08-30)

Primary citation

Kumar, A.O.,Swenson, M.C.,Benning, M.M.,Kielkopf, C.L.
Structure of the central RNA recognition motif of human TIA-1 at 1.95A resolution.
Biochem.Biophys.Res.Commun., 367:813-819, 2008

PubMed Abstract: 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.

PubMed: 18201561
DOI: 10.1016/j.bbrc.2008.01.027

Experimental method

X-RAY DIFFRACTION (1.95 Å)