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- W3146961733 abstract "Abstract Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor that maintains Ca 2+ homeostasis in serum. Here, we present the cryo-electron microscopy structures of the CaSR in the inactive and active states. Complemented with previously reported crystal structures of CaSR extracellular domains, it suggests that there are three distinct conformations: inactive, intermediate and active state during the activation. We used a negative allosteric nanobody to stabilize the CaSR in the fully inactive state and found a new binding site for Ca 2+ ion that acts as a composite agonist with L-amino acid to stabilize the closure of active Venus flytraps. Our data shows that the agonist binding leads to the compaction of the dimer, the proximity of the cysteine-rich domains, the large-scale transitions of 7-transmembrane domains, and the inter-and intrasubunit conformational changes of 7-transmembrane domains to accommodate the downstream transducers. Our results reveal the structural basis for activation mechanisms of the CaSR." @default.
- W3146961733 created "2021-04-13" @default.
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- W3146961733 date "2021-03-31" @default.
- W3146961733 modified "2023-09-23" @default.
- W3146961733 title "Structural insights into the activation of human calcium-sensing receptor" @default.
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- W3146961733 doi "https://doi.org/10.1101/2021.03.30.437720" @default.
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