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
- 25 March 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 280 (2), 207-210
- https://doi.org/10.1016/0014-5793(91)80294-d
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 suggest 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.Keywords
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