Contribution of serine residues to constitutive and agonist-induced signaling via the D2S dopamine receptor: evidence for multiple, agonist-specific active conformations.

@article{Wiens1998ContributionOS,
  title={Contribution of serine residues to constitutive and agonist-induced signaling via the D2S dopamine receptor: evidence for multiple, agonist-specific active conformations.},
  author={B. L. Wiens and C. Nelson and K. Neve},
  journal={Molecular pharmacology},
  year={1998},
  volume={54 2},
  pages={
          435-44
        }
}
  • B. L. Wiens, C. Nelson, K. Neve
  • Published 1998
  • Medicine, Biology
  • Molecular pharmacology
  • Dopamine D2 receptors contain a cluster of serine residues in the fifth transmembrane domain that contribute to activation of the receptor as well as to the binding of agonists. We used rat D2S dopamine receptor mutants, each containing a serine-to-alanine substitution (S193A, S194A, S197A), to investigate the mechanism through which these residues affect activation of the receptor. Activation of the mutant receptor S194A was abolished in an agonist-dependent manner, such that dopamine no… CONTINUE READING
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