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Updated: Jun 21, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Backbone and sidechain 1H, 15N, and 13C assignments of the human eIF5A
Jinqiao Yuan1, Nan Jiang, Changwen Jin
1National Center of Biomedical Analysis, Beijing, 100850, People's Republic of China.
Abstract:
The putative translation initiation factor eIF5A is essential for cell viability and is highly conserved from archaebacteria to mammals. This factor is the only cellular protein that undergoes an essential posttranslational modification dependent on the polyamine spermidine, called hypusination. Although this protein may be involved in many important physiological functions, the precise molecular functions of eIF-5A remain to be clarified. To determine the solution structure and the protein interactions of eIF5A with its potential substrates, we performed NMR studies. Here, we report the nearly complete assignment of the eIF5A.
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