Hydrophobic residues in helix 8 of cannabinoid receptor 1 are critical for structural and functional properties.

@article{Ahn2010HydrophobicRI,
  title={Hydrophobic residues in helix 8 of cannabinoid receptor 1 are critical for structural and functional properties.},
  author={Kwang H. Ahn and Akiko Nishiyama and Dale F. Mierke and Debra A. Kendall},
  journal={Biochemistry},
  year={2010},
  volume={49 3},
  pages={502-11}
}
In addition to the heptahelical transmembrane domain shared by all G protein-coupled receptors (GPCRs), many class A GPCRs adopt a helical domain, termed helix 8, in the membrane-proximal region of the C terminus. We investigated the role of residues in the hydrophobic and hydrophilic faces of amphiphilic helix 8 of human cannabinoid receptor 1 (CB1). To differentiate between a role for specific residues and global features, we made two key mutants: one involving replacement of the highly… CONTINUE READING
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