Agonist-bound structure of the human P2Y12 receptor

  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},
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
Related Discussions
This paper has been referenced on Twitter 12 times. VIEW TWEETS


Publications citing this paper.
Showing 1-10 of 57 extracted citations

An Update on P2Y13 Receptor Signalling and Function.

Advances in experimental medicine and biology • 2017
View 3 Excerpts
Highly Influenced

Successful Strategies to Determine High-Resolution Structures of GPCRs.

Trends in pharmacological sciences • 2016
View 4 Excerpts
Highly Influenced

Chemical Diversity in the G Protein-Coupled Receptor Superfamily.

Trends in pharmacological sciences • 2018
View 9 Excerpts


Publications referenced by this paper.
Showing 1-10 of 32 references

Structure of the human P2Y12 receptor in complex with an antithrombotic drug

K Zhang

Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist

K Haga

Similar Papers

Loading similar papers…