The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5

J Mol Biol. 2006 Jul 7;360(2):457-65. doi: 10.1016/j.jmb.2006.05.021. Epub 2006 May 24.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites / genetics
  • Chromatography, Gel
  • Crystallography, X-Ray
  • Eukaryotic Initiation Factor-5 / chemistry*
  • Humans
  • Molecular Sequence Data
  • Mutation / genetics
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Temperature


  • Eukaryotic Initiation Factor-5

Associated data

  • PDB/2IU1