1H, 13C, and 15N backbone chemical shift assignments of 4E-BP144-87 and 4E-BP144-87 bound to eIF4E

Biomol NMR Assign. 2017 Oct;11(2):187-191. doi: 10.1007/s12104-017-9744-9. Epub 2017 Jun 6.


The eukaryotic translational initiation factor 4G (eIF4G) interacts with the cap-binding protein eIF4E through a consensus binding motif, Y(X)4LΦ (where X is any amino acid and Φ is a hydrophobic residue). 4E binding proteins (4E-BPs), which also contain a Y(X)4LΦ motif, regulate the eIF4E/eIF4G interaction. The non- or minimally-phosphorylated form of 4E-BP1 binds eIF4E, preventing eIF4E from interacting with eIF4G, thus inhibiting translation initiation. 4EGI-1, a small molecule inhibitor of the eIF4E/eIF4G interaction that is under investigation as a novel anti-cancer drug, has a dual activity; it disrupts the eIF4E/eIF4G interaction and stabilizes the binding of 4E-BP1 to eIF4E. Here, we report the complete backbone NMR resonance assignment of an unliganded 4E-BP1 fragment (4E-BP144-87). We also report the near complete backbone assignment of the same fragment in complex to eIF4E/m7GTP (excluding the assignment of the last C-terminus residue, D87). The chemical shift data constitute a prerequisite to understanding the mechanism of action of translation initiation inhibitors, including 4EGI-1, that modulate the eIF4E/4E-BP1 interaction.

Keywords: 4E-BP1; NMR assignment; Translation initiation; eIF4E.

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism*
  • Cell Cycle Proteins
  • Eukaryotic Initiation Factor-4E / metabolism*
  • Eukaryotic Initiation Factors
  • Humans
  • Nuclear Magnetic Resonance, Biomolecular*
  • Phosphoproteins / chemistry*
  • Phosphoproteins / metabolism*
  • Protein Binding


  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • Cell Cycle Proteins
  • Eif4ebp1 protein, mouse
  • Eukaryotic Initiation Factor-4E
  • Eukaryotic Initiation Factors
  • Phosphoproteins