3mei | pdb_00003mei

Regulatory motif from the thymidylate synthase mRNA

spinqualitylabelsall models 3mei, resolution 1.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3mei is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG NonStd Res: 5BU Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Structure of an RNA dimer of a regulatory element from human thymidylate synthase mRNA.,Dibrov S, McLean J, Hermann T Acta Crystallogr D Biol Crystallogr. 2011 Feb;67(Pt 2):97-104. Epub 2011, Jan 8. PMID:21245530 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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