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7TS0

Cryo-EM structure of corticotropin releasing factor receptor 2 bound to Urocortin 1 and coupled with heterotrimeric Go protein

Summary for 7TS0
Entry DOI10.2210/pdb7ts0/pdb
EMDB information26103 26104
DescriptorCorticotropin-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 Keywordsgpcr, corticotropin releasing factor receptor 2, urocortin 1, go protein, signaling protein
Biological sourceHomo sapiens (human)
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Total number of polymer chains6
Total formula weight186297.20
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 citationZhao, 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: 36335102
DOI: 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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