7WU3
 
 | | Cryo-EM structure of the adhesion GPCR ADGRF1 in complex with miniGs | | Descriptor: | Adhesion G-protein coupled receptor F1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, ... | | Authors: | Qu, X, Qiu, N, Wang, M, Zhao, Q, Wu, B. | | Deposit date: | 2022-02-05 | | Release date: | 2022-04-27 | | Last modified: | 2022-05-11 | | Method: | ELECTRON MICROSCOPY (3.1 Å) | | Cite: | Structural basis of tethered agonism of the adhesion GPCRs ADGRD1 and ADGRF1.
Nature, 604, 2022
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7WU4
 | | Cryo-EM structure of the adhesion GPCR ADGRF1 in complex with miniGi | | Descriptor: | Adhesion G-protein coupled receptor F1, CHOLESTEROL, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, ... | | Authors: | Qu, X, Qiu, N, Wang, M, Zhao, Q, Wu, B. | | Deposit date: | 2022-02-05 | | Release date: | 2022-04-27 | | Last modified: | 2022-05-11 | | Method: | ELECTRON MICROSCOPY (3.4 Å) | | Cite: | Structural basis of tethered agonism of the adhesion GPCRs ADGRD1 and ADGRF1.
Nature, 604, 2022
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7WU5
 | | Cryo-EM structure of the adhesion GPCR ADGRF1(H565A/T567A) in complex with miniGi | | Descriptor: | Adhesion G-protein coupled receptor F1, CHOLESTEROL, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, ... | | Authors: | Qu, X, Qiu, N, Wang, M, Zhao, Q, Wu, B. | | Deposit date: | 2022-02-05 | | Release date: | 2022-04-27 | | Last modified: | 2022-05-11 | | Method: | ELECTRON MICROSCOPY (3 Å) | | Cite: | Structural basis of tethered agonism of the adhesion GPCRs ADGRD1 and ADGRF1.
Nature, 604, 2022
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7WU2
 | | Cryo-EM structure of the adhesion GPCR ADGRD1 in complex with miniGs | | Descriptor: | Adhesion G-protein coupled receptor D1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, ... | | Authors: | Qu, X, Qiu, N, Wang, M, Zhao, Q, Wu, B. | | Deposit date: | 2022-02-05 | | Release date: | 2022-04-27 | | Last modified: | 2022-05-11 | | Method: | ELECTRON MICROSCOPY (2.8 Å) | | Cite: | Structural basis of tethered agonism of the adhesion GPCRs ADGRD1 and ADGRF1.
Nature, 604, 2022
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