Agonist-bound structure of the human P2Y12 receptor

@inproceedings{Zhang2014AgonistboundSO,
  title={Agonist-bound structure of the human P2Y12 receptor},
  author={Jin Zhang and Kaihua Zhang and Zhan-guo Gao and Silvia Paoletta and Dong Zhang and Gye Won Han and Ting Li and Limin Ma and Wenru Zhang and Christa E. M{\"u}ller and Huaiyu Yang and Hualiang Jiang and Vadim Cherezov and Vsevolod Katritch and Kenneth A. Jacobson and Raymond C. Stevens and Beili Wu and Qiang Zhao},
  booktitle={Nature},
  year={2014}
}
The P2Y12 receptor (P2Y12R), one of eight members of the P2YR family expressed in humans, is one of the most prominent clinical drug targets for inhibition of platelet aggregation. Although mutagenesis and modelling studies of the P2Y12R provided useful insights into ligand binding, the agonist and antagonist recognition and function at the P2Y12R remain poorly understood at the molecular level. Here we report the structures of the human P2Y12R in complex with the full agonist 2-methylthio… CONTINUE READING
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