Structure and ligand-binding mechanism of the human OX1 and OX2 orexin receptors

@article{Yin2016StructureAL,
  title={Structure and ligand-binding mechanism of the human OX1 and OX2 orexin receptors},
  author={Jie Yin and Kerim Babaoglu and Chad A. Brautigam and Lindsay Clark and Zhenhua Shao and Thomas H. Scheuermann and Charles Harrell and Anthony L Gotter and Anthony J. Roecker and Christopher J Winrow and John Renger and Paul J. Coleman and Daniel M Rosenbaum},
  journal={Nature Structural &Molecular Biology},
  year={2016},
  volume={23},
  pages={293-299}
}

• Jie Yin, Kerim Babaoglu, +10 authors Daniel M Rosenbaum
• Published in Nature Structural &Molecular Biology 2016
• DOI:10.1038/nsmb.3183

The orexin (also known as hypocretin) G protein–coupled receptors (GPCRs) regulate sleep and other behavioral functions in mammals, and are therapeutic targets for sleep and wake disorders. The human receptors hOX1R and hOX2R, which are 64% identical in sequence, have overlapping but distinct physiological functions and potential therapeutic profiles. We determined structures of hOX1R bound to the OX1R-selective antagonist SB-674042 and the dual antagonist suvorexant at 2.8-Å and 2.75… CONTINUE READING

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