Structural-functional analysis of the third transmembrane domain of the corticotropin-releasing factor type 1 receptor: role in activation and allosteric antagonism.

@article{Spyridaki2014StructuralfunctionalAO,
  title={Structural-functional analysis of the third transmembrane domain of the corticotropin-releasing factor type 1 receptor: role in activation and allosteric antagonism.},
  author={Katerina Spyridaki and Minos-Timotheos Matsoukas and Arnau Cordom{\'i} and Kostas Gkountelias and Maria Papadokostaki and Thomas M. Mavromoustakos and Diomedes E. Logothetis and Andrew N. Margioris and Leonardo Pardo and George Liapakis},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 27},
  pages={18966-77}
}
The corticotropin-releasing factor (CRF) type 1 receptor (CRF1R) for the 41-amino acid peptide CRF is a class B G protein-coupled receptor, which plays a key role in the response of our body to stressful stimuli and the maintenance of homeostasis by regulating neural and endocrine functions. CRF and related peptides, such as sauvagine, bind to the extracellular regions of CRF1R and activate the receptor. In contrast, small nonpeptide antagonists, which are effective against stress-related… CONTINUE READING
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