Crystal structures of 7-methylguanosine 5'-triphosphate (m(7)GTP)- and P(1)-7-methylguanosine-P(3)-adenosine-5',5'-triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation factor 4E: biological importance of the C-terminal flexible region.

@article{Tomoo2002CrystalSO,
  title={Crystal structures of 7-methylguanosine 5'-triphosphate (m(7)GTP)- and P(1)-7-methylguanosine-P(3)-adenosine-5',5'-triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation factor 4E: biological importance of the C-terminal flexible region.},
  author={Koji Tomoo and Xu Shen and Koumei Okabe and Yoshiaki Nozoe and Shoichi Fukuhara and Shigenobu Morino and Toshimasa Ishida and Taizo Taniguchi and Hiroshi Hasegawa and Akira Terashima and Masahiro Sasaki and Yoshio Katsuya and Kunihiro Kitamura and Hiroshi Miyoshi and Masahide Ishikawa and K. T. Miura},
  journal={The Biochemical journal},
  year={2002},
  volume={362 Pt 3},
  pages={539-44}
}
The crystal structures of the full-length human eukaryotic initiation factor (eIF) 4E complexed with two mRNA cap analogues [7-methylguanosine 5'-triphosphate (m(7)GTP) and P(1)-7-methylguanosine-P(3)-adenosine-5',5'-triphosphate (m(7)GpppA)] were determined at 2.0 A resolution (where 1 A=0.1 nm). The flexibility of the C-terminal loop region of eIF4E complexed with m(7)GTP was significantly reduced when complexed with m(7)GpppA, suggesting the importance of the second nucleotide in the mRNA… CONTINUE READING