From molecular details of the interplay between transmembrane helices of the thyrotropin receptor to general aspects of signal transduction in family a G-protein-coupled receptors (GPCRs).

@article{Kleinau2011FromMD,
  title={From molecular details of the interplay between transmembrane helices of the thyrotropin receptor to general aspects of signal transduction in family a G-protein-coupled receptors (GPCRs).},
  author={Gunnar Kleinau and Inna Hoyer and Annika Kreuchwig and Ann-Karin Haas and Claudia Rutz and Jens Furkert and Catherine L. Worth and Gerd Krause and Ralf Schuelein},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 29},
  pages={25859-71}
}
Transmembrane helices (TMHs) 5 and 6 are known to be important for signal transduction by G-protein-coupled receptors (GPCRs). Our aim was to characterize the interface between TMH5 and TMH6 of the thyrotropin receptor (TSHR) to gain molecular insights into aspects of signal transduction and regulation. A proline at TMH5 position 5.50 is highly conserved in family A GPCRs and causes a twist in the helix structure. Mutation of the TSHR-specific alanine (Ala-593⁵·⁵⁰) at this position to proline… CONTINUE READING

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