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

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

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  • 2006-06-20
Published in:
  • 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
English 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.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/1151
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