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Combination of Trp and Glu residues for recognition of mRNA cap structure Analysis of m 7 G base recognition site of human cap binding protein (IF‐4E) by site‐directed mutagenesis
Author(s) -
Ueda Hitoshi,
Iyo Hiromi,
Doi Mitsunobu,
Inoue Masatoshi,
Ishida Toshimasa,
Morioka Hiroshi,
Tanaka Toshiki,
Nishikawa Satoshi,
Uesugi Seiichi
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80294-d
Subject(s) - binding site , chemistry , mutant , stereochemistry , hydrogen bond , stacking , biochemistry , gene , molecule , organic chemistry
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 m 7 G 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.