7TS0
Cryo-EM structure of corticotropin releasing factor receptor 2 bound to Urocortin 1 and coupled with heterotrimeric Go protein
Summary for 7TS0
Entry DOI | 10.2210/pdb7ts0/pdb |
EMDB information | 26103 26104 |
Descriptor | Corticotropin-releasing factor receptor 2,Corticotropin-releasing factor receptor 2,Corticotropin-releasing factor receptor 2,Corticotropin-releasing factor receptor 2,Human corticotropin releasing factor receptor 2, Urocortin, Dominant negative Go alpha subunit, ... (6 entities in total) |
Functional Keywords | gpcr, corticotropin releasing factor receptor 2, urocortin 1, go protein, signaling protein |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 6 |
Total formula weight | 186297.20 |
Authors | Zhao, L.-H.,Lin, J.,Mao, C.,Zhou, X.E.,Ji, S.,Shen, D.,Xiao, P.,Melcher, K.,Zhang, Y.,Yu, X.,Xu, H.E. (deposition date: 2022-01-31, release date: 2022-11-09, Last modification date: 2025-05-14) |
Primary citation | Zhao, L.H.,Lin, J.,Ji, S.Y.,Zhou, X.E.,Mao, C.,Shen, D.D.,He, X.,Xiao, P.,Sun, J.,Melcher, K.,Zhang, Y.,Yu, X.,Xu, H.E. Structure insights into selective coupling of G protein subtypes by a class B G protein-coupled receptor. Nat Commun, 13:6670-6670, 2022 Cited by PubMed Abstract: The ability to couple with multiple G protein subtypes, such as G, G, or G, by a given G protein-coupled receptor (GPCR) is critical for many physiological processes. Over the past few years, the cryo-EM structures for all 15 members of the medically important class B GPCRs, all in complex with G protein, have been determined. However, no structure of class B GPCRs with G has been solved to date, limiting our understanding of the precise mechanisms of G protein coupling selectivity. Here we report the structures of corticotropin releasing factor receptor 2 (CRF2R) bound to Urocortin 1 (UCN1), coupled with different classes of heterotrimeric G proteins, G and G. We compare these structures with the structure of CRF2R in complex with G to uncover the structural differences that determine the selective coupling of G protein subtypes by CRF2R. These results provide important insights into the structural basis for the ability of CRF2R to couple with multiple G protein subtypes. PubMed: 36335102DOI: 10.1038/s41467-022-33851-3 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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