Backbone and sidechain 1H, 15N, and 13C assignments of the human eIF5A.
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.
Yuan
Jinqiao
J
National Center of Biomedical Analysis, Beijing, 100850, People's Republic of China.
Jiang
Nan
N
Jin
Changwen
C
Zhang
Xuemin
X
Yan
Xianzhong
X
D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes / Q000737:chemistry; D010448:Peptide Initiation Factors / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011522:Protons; D016601:RNA-Binding Proteins / Q000737:chemistry*; D000097574:Eukaryotic Translation Initiation Factor 5A
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D010448:Peptide Initiation Factors; D021122:Protein Subunits; D011522:Protons; D016601:RNA-Binding Proteins; D000097574:Eukaryotic Translation Initiation Factor 5A