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The cystic fibrosis mutation, ΔF508, disrupts CFTR biosynthesis. ΔF508 protein resembles an early intermediate in wild type folding, but fails to adopt a mature conformation and hence cannot escape the ER.
A new structure brings into sharp focus the structural basis for G–C base pair recognition by small ligands in the minor groove of DNA. At the same time the ability to distinguish specific sequences moves another major step forward through introduction of a new ligand modification.
The co-crystal structure of VP39 recognizing a eukaryotic mRNA reveals non-specifc protein–RNA interactions that saturate the polynucleotide backbone with contacts while ignoring the bases.
A new RNA aptamer–protein co-crystal surprisingly shows that bacteriophage MS2 coat protein uses a similar set of contacts to bind both a native RNA ligand and an RNA hairpin with a different secondary structure.
