4phy | pdb_00004phy

Functional conservation despite structural divergence in ligand-responsive RNA switches

spinqualitylabelsall models 4phy, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4phy is a 2 chain structure with sequence from Senecavirus A. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: ACT, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed An internal ribosome entry site (IRES) initiates protein synthesis in RNA viruses, including the hepatitis C virus (HCV). We have discovered ligand-responsive conformational switches in viral IRES elements. Modular RNA motifs of greatly distinct sequence and local secondary structure have been found to serve as functionally conserved switches involved in viral IRES-driven translation and may be captured by identical cognate ligands. The RNA motifs described here constitute a new paradigm for ligand-captured switches that differ from metabolite-sensing riboswitches with regard to their small size, as well as the intrinsic stability and structural definition of the constitutive conformational states. These viral RNA modules represent the simplest form of ligand-responsive mechanical switches in nucleic acids. Functional conservation despite structural divergence in ligand-responsive RNA switches.,Boerneke MA, Dibrov SM, Gu J, Wyles DL, Hermann T Proc Natl Acad Sci U S A. 2014 Nov 11;111(45):15952-7. doi:, 10.1073/pnas.1414678111. Epub 2014 Oct 27. PMID:25349403 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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