Can Cao
Chinese Academy of Sciences
15 Papers
24 Citations
Can Cao is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: G protein-coupled receptor & Chemistry. The author has an hindex of 7, co-authored 10 publications.
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Papers
Structure of the glucagon receptor in complex with a glucagon analogue
Haonan Zhang,Anna Qiao,Linlin Yang,Ned Van Eps,Klaus Stensgaard Frederiksen,Dehua Yang,Antao Dai,Xiaoqing Cai,Hui Zhang,Cuiying Yi,Can Cao,Lingli He,Huaiyu Yang,Jesper Lau,Oliver P. Ernst,Michael A. Hanson,Raymond C. Stevens,Ming-Wei Wang,Steffen Reedtz-Runge,Hualiang Jiang,Qiang Zhao,Beili Wu +21 more
TL;DR: This work reports the 3.0 Å-resolution crystal structure of the full-length human glucagon receptor (GCGR) in complex with a glucagon analogue and partial agonist, NNC1702, and proposes a dual-binding-site trigger model for GCGR activation that extends the understanding of the previously established two-domain peptide-binding model of class B GPCRs.
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Signaling snapshots of a serotonin receptor activated by the prototypical psychedelic LSD
Can Cao,Ximena Barros-Álvarez,Shicheng Zhang,Kuglae Kim,Marc A. Dämgen,Ouliana Panova,Carl-Mikael Suomivuori,Jonathan F. Fay,Xiaofang Zhong,Brian E. Krumm,Ryan H. Gumpper,Alpay B. Seven,Michael J. Robertson,Nevan J. Krogan,Ruth Hüttenhain,David E. Nichols,Ron O. Dror,Georgios Skiniotis,Bryan L. Roth +18 more
TL;DR: In this paper , the authors determined the cryo-EM structures of LSD-bound HTR2B in the transducer-free, Gq-protein-coupled, and β-arrestin-1-cooperative states, which provided comprehensive molecular insights into the signaling mechanisms of the prototypical LSD and accelerate the discovery of novel psychedelic drugs.
92
GPCR activation: protonation and membrane potential
TL;DR: This work has identified a potential conformational switch around the conserved Asp2.50, which consistently shows distinct conformations between inactive and active states and proposes an energy-coupling mechanism, in which the interaction between a charge change of the GPCR protein and the membrane potential of the living cell plays a key role for G PCR activation.
Cryo-electron microscopy structure of human ABCB6 transporter.
TL;DR: The structure of ABCB6 unravels the architecture of a full‐length ABCB transporter that harbors two N‐terminal transmembrane domains which is indispensable for its ATPase activity in the authors' in vitro assay.
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Crystal structure of dopamine receptor D4 bound to the subtype selective ligand, L745870.
TL;DR: The 3.5-angstrom crystal structure of mouse dopamine receptor D4 complexed with a subtype-selective antagonist, L745870, reveals a secondary binding pocket extended from the orthosteric ligand-binding pocket to a DRD4-specific crevice located between transmembrane helices 2 and 3.
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