Spectroscopic evidence for interaction between transmembrane helices 3 and 5 in rhodopsin.

@article{Beck1998SpectroscopicEF,
  title={Spectroscopic evidence for interaction between transmembrane helices 3 and 5 in rhodopsin.},
  author={Mareike Beck and Thomas P. Sakmar and Friedrich Siebert},
  journal={Biochemistry},
  year={1998},
  volume={37 20},
  pages={7630-9}
}
Recent molecular models of rhodopsin (Rho) propose a specific interaction between transmembrane (TM) helices 3 and 5, which appears to be mediated by amino acid residues Glu122 and His211 on TM helices 3 and 5, respectively. To test this proposed interaction, four single-site histidine replacement mutants (H100N, H152N, H211N, and H211F), two single-site glutamic acid replacement mutants (E122Q and E122A), and three double-site replacement mutants (E122Q/H211F, E122Q/H211N, and E122A/H211F) of… CONTINUE READING

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