7XX8
Solution structure of RRM1 of Human SART3
Summary for 7XX8
| Entry DOI | 10.2210/pdb7xx8/pdb |
| Descriptor | Squamous cell carcinoma antigen recognized by T-cells 3 (1 entity in total) |
| Functional Keywords | rna binding protein rna recognition motif rna processing, rna binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 10738.19 |
| Authors | Kim, I.,Bang, K.M.,Park, C.,Kim, N.K.,Suh, J.Y. (deposition date: 2022-05-29, release date: 2023-08-30, Last modification date: 2025-10-29) |
| Primary citation | Kim, I.,Bang, K.M.,An, S.Y.,Park, C.,Shin, J.Y.,Kim, Y.,Song, H.K.,Suh, J.Y.,Kim, N.K. Structural investigation of human U6 snRNA recognition by spliceosomal recycling factor SART3 RNA recognition motifs. Febs J., 2025 Cited by PubMed Abstract: Human spliceosome-associated factor 3, SART3, is a key factor in spliceosome recycling and engages with U6 small nuclear RNA (snRNA) to promote the formation of the U4/U6 small nuclear ribonucleoprotein complex. Unlike its counterpart U4/U6 snRNA-associated-splicing factor PRP24 (Prp24) from Saccharomyces cerevisiae, which uses four RNA recognition motifs (RRMs) for the U6 snRNA interaction, SART3 has two RRMs at its C terminus. Here, we demonstrate that SART3 binds U6 snRNA as a dimer, and four RRM subunits recognize the asymmetric bulge of U6 snRNA. SART3 RRMs adopt a tandem βαββαβ motif of the canonical RRM fold to interact with the U6 bulge region via a conserved electropositive surface. We identified the cognate U6 elements that specifically bind SART3 RRM1, which is distinct from the Prp24-U6 interactions in yeast. Our findings suggest a divergent RRM binding mechanism for U6 snRNA recognition during spliceosome assembly and recycling. PubMed: 41046346DOI: 10.1111/febs.70275 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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