3MEI
Regulatory motif from the thymidylate synthase mRNA
Summary for 3MEI
| Entry DOI | 10.2210/pdb3mei/pdb |
| Descriptor | RNA (5'-R(*CP*CP*GP*CP*CP*GP*CP*GP*CP*CP*AP*(5BU)P*GP*CP*CP*UP*GP*UP*GP*GP*CP*GP*G)-3'), MAGNESIUM ION (3 entities in total) |
| Functional Keywords | s-turn, c-c base pair, rna |
| Total number of polymer chains | 2 |
| Total formula weight | 15002.15 |
| Authors | Dibrov, S.,McLean, J.,Hermann, T. (deposition date: 2010-03-31, release date: 2011-01-26, Last modification date: 2024-02-21) |
| Primary citation | Dibrov, S.,McLean, J.,Hermann, T. Structure of an RNA dimer of a regulatory element from human thymidylate synthase mRNA. Acta Crystallogr.,Sect.D, 67:97-104, 2011 Cited by PubMed Abstract: A sequence around the start codon of the mRNA of human thymidylate synthase (TS) folds into a secondary-structure motif in which the initiation site is sequestered in a metastable hairpin. Binding of the protein to its own mRNA at the hairpin prevents the production of TS through a translation-repression feedback mechanism. Stabilization of the mRNA hairpin by other ligands has been proposed as a strategy to reduce TS levels in anticancer therapy. Rapidly proliferating cells require high TS activity to maintain the production of thymidine as a building block for DNA synthesis. The crystal structure of a model oligonucleotide (TS1) that represents the TS-binding site of the mRNA has been determined. While fluorescence studies showed that the TS1 RNA preferentially adopts a hairpin structure in solution, even at high RNA concentrations, an asymmetric dimer of two hybridized TS1 strands was obtained in the crystal. The TS1 dimer contains an unusual S-turn motif that also occurs in the `off' state of the human ribosomal decoding site RNA. PubMed: 21245530DOI: 10.1107/S0907444910050900 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.968 Å) |
Structure validation
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