title: The unfolding story of polypeptide release factors.
abstract: Two recent cryo-EM reconstructions of the ribosome-bound release factor RF2 reveal an open, tri-lobed shape of RF2, in contrast to the comma-shaped molecule seen in the crystal structure. This indicates that RF2 undergoes a conformational change upon binding to the ribosome. Moreover, RF2 does not seem to be a molecular mimic of tRNA as is the case for elongation factor G.
authors.affiliation: Department of Molecular Biology, Aarhus University, DK-8000 Aarhus C, Denmark.
authors.forename: Morten
authors.initials: M
authors.lastname: Kjeldgaard
mesh_terms: D006801:Humans; D008958:Models, Molecular; D010454:Peptide Termination Factors / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012270:Ribosomes / Q000378:metabolism
chemical_list: D010454:Peptide Termination Factors; C041460:peptide chain termination release factor 2