2O3D
Structure of human SF2/ASF RNA recognition motif 2 (RRM2)
Summary for 2O3D
| Entry DOI | 10.2210/pdb2o3d/pdb |
| NMR Information | BMRB: 7301 |
| Descriptor | Splicing factor, arginine/serine-rich 1 (1 entity in total) |
| Functional Keywords | rrm domain, rna binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q07955 |
| Total number of polymer chains | 1 |
| Total formula weight | 12930.45 |
| Authors | Tintaru, A.M.,Hautbergue, G.M.,Hounslow, A.M.,Lian, L.Y.,Craven, C.J.,Wilson, S.A. (deposition date: 2006-12-01, release date: 2007-10-16, Last modification date: 2023-12-27) |
| Primary citation | Tintaru, A.M.,Hautbergue, G.M.,Hounslow, A.M.,Hung, M.L.,Lian, L.Y.,Craven, C.J.,Wilson, S.A. Structural and functional analysis of RNA and TAP binding to SF2/ASF. Embo Rep., 8:756-762, 2007 Cited by PubMed Abstract: The serine/arginine-rich (SR) protein splicing factor 2/alternative splicing factor (SF2/ASF) has a role in splicing, stability, export and translation of messenger RNA. Here, we present the structure of the RNA recognition motif (RRM) 2 from SF2/ASF, which has an RRM fold with a considerably extended loop 5 region, containing a two-stranded beta-sheet. The loop 5 extension places the previously identified SR protein kinase 1 docking sequence largely within the RRM fold. We show that RRM2 binds to RNA in a new way, by using a tryptophan within a conserved SWQLKD motif that resides on helix alpha1, together with amino acids from strand beta2 and a histidine on loop 5. The linker connecting RRM1 and RRM2 contains arginine residues, which provide a binding site for the mRNA export factor TAP, and when TAP binds to this region it displaces RNA bound to RRM2. PubMed: 17668007DOI: 10.1038/sj.embor.7401031 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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