Bieniossek C Schütz P Bumann M Limacher A Uson I Baumann U 2006 The carboxy-terminal domain (CTD) of eukaryotic initiation factor 5 (eIF5) plays a central role in the formation of the multifactor complex (MFC), an important intermediate for the 43 S pre-initiation complex assembly. The IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-beta, and eIF3c, thus forming together with eIF2 bound Met-tRNA(i)(Met) the MFC. In this work we present the high resolution crystal structure of eIF5-CTD. This domain of the protein is exclusively composed out of alpha-helices and is homologous to the carboxy-terminal domain of eIF2B-epsilon (eIF2Bepsilon-CTD). The most striking difference in the two structures is an additional carboxy-terminal helix in eIF5. The binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure. eIF2-beta and eIF3 bind to non-overlapping patches of negative and positive electrostatic potential, respectively. https://sonar.ch/global/documents/1151 eng info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmb.2006.05.021 info:eu-repo/semantics/altIdentifier/pmid/16781736 Journal of molecular biology. - 2006 Amino Acid Sequence Binding Sites Chromatography, Gel Crystallography, X-Ray Eukaryotic Initiation Factor-5 Humans Molecular Sequence Data Mutation Protein Structure, Tertiary Sequence Alignment Temperature The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5. http://purl.org/coar/resource_type/c_6501