6E67
Structure of beta2 adrenergic receptor fused to a Gs peptide
Summary for 6E67
Entry DOI | 10.2210/pdb6e67/pdb |
Descriptor | Beta-2 adrenergic receptor,Endolysin,Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,Beta-2 adrenergic receptor chimera, 8-[(1R)-2-{[1,1-dimethyl-2-(2-methylphenyl)ethyl]amino}-1-hydroxyethyl]-5-hydroxy-2H-1,4-benzoxazin-3(4H)-one (2 entities in total) |
Functional Keywords | g protein coupled receptor, membrane protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 2 |
Total formula weight | 121057.96 |
Authors | Liu, X.,Xu, X.,Hilger, D.,Tiemann, J.,Liu, H.,Du, Y.,Hirata, K.,Sun, X.,Guixa-Gonzalez, R.,Mathiesen, J.,Hildebrand, P.,Kobilka, B. (deposition date: 2018-07-24, release date: 2019-06-05, Last modification date: 2024-11-20) |
Primary citation | Liu, X.,Xu, X.,Hilger, D.,Aschauer, P.,Tiemann, J.K.S.,Du, Y.,Liu, H.,Hirata, K.,Sun, X.,Guixa-Gonzalez, R.,Mathiesen, J.M.,Hildebrand, P.W.,Kobilka, B.K. Structural Insights into the Process of GPCR-G Protein Complex Formation. Cell, 177:1243-1251.e12, 2019 Cited by PubMed Abstract: The crystal structure of the β2-adrenergic receptor (β2AR) bound to the G protein adenylyl cyclase stimulatory G protein (Gs) captured the complex in a nucleotide-free state (β2AR-Gs). Unfortunately, the β2AR-Gs complex does not provide a clear explanation for G protein coupling specificity. Evidence from several sources suggests the existence of a transient complex between the β2AR and GDP-bound Gs protein (β2AR-Gs) that may represent an intermediate on the way to the formation of β2AR-Gs and may contribute to coupling specificity. Here we present a structure of the β2AR in complex with the carboxyl terminal 14 amino acids from Gαs along with the structure of the GDP-bound Gs heterotrimer. These structures provide evidence for an alternate interaction between the β2AR and Gs that may represent an intermediate that contributes to Gs coupling specificity. PubMed: 31080070DOI: 10.1016/j.cell.2019.04.021 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.7 Å) |
Structure validation
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