Combination of Trp and Glu residues for recognition of mRNA cap structure. Analysis of m7G base recognition site of human cap binding protein (IF-4E) by site-directed mutagenesis.
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Ueda H, Iyo H, Doi M, Inoue M, Ishida T, Morioka H, Tanaka T, Nishikawa S, Uesugi S
Combination of Trp and Glu residues for recognition of mRNA cap structure. Analysis of m7G base recognition site of human cap binding protein (IF-4E) by site-directed mutagenesis.
FEBS Lett. 1991 Mar 25;280(2):207-10.
- PubMed ID
- 1672854 [ View in PubMed]
- Abstract
Four mutants of the human cap binding protein (hCBP), in which Trp-102, Glu-103, Asp-104 or Glu-105 was changed to the aliphatic Leu or Ala, were prepared, and their cap binding abilities were examined. Cap binding abilities of two mutants, W102L (Trp-102----Leu) and E105A (Glu-105----Ala), were significantly decreased in comparison with the wild-type hCBP. This result suggests that Trp-102 and Glu-105 are both necessary for the cap binding, and the most probable binding mode with the m7G of cap structure is the combination of the stacking by Trp-102 and the hydrogen-bond pairing by Glu-105, as was already proposed from the model studies.