Structural highlights
Function
GBG2_BOVIN Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Publication Abstract from PubMed
The beta(1)-adrenergic receptor (beta(1)-AR) can activate two families of G proteins. When coupled to Gs, beta(1)-AR increases cardiac output, and coupling to Gi leads to decreased responsiveness in myocardial infarction. By comparative structural analysis of turkey beta(1)-AR complexed with either Gi or Gs, we investigate how a single G-protein-coupled receptor simultaneously signals through two G proteins. We find that, although the critical receptor-interacting C-terminal alpha5-helices on Galpha(i) and Galpha(s) interact similarly with beta(1)-AR, the overall interacting modes between beta(1)-AR and G proteins vary substantially. Functional studies reveal the importance of the differing interactions and provide evidence that the activation efficacy of G proteins by beta(1)-AR is determined by the entire three-dimensional interaction surface, including intracellular loops 2 and 4 (ICL2 and ICL4).
Structural basis and mechanism of activation of two different families of G proteins by the same GPCR.,Alegre KO, Paknejad N, Su M, Lou JS, Huang J, Jordan KD, Eng ET, Meyerson JR, Hite RK, Huang XY Nat Struct Mol Biol. 2021 Nov;28(11):936-944. doi: 10.1038/s41594-021-00679-2. , Epub 2021 Nov 10. PMID:34759376[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Alegre KO, Paknejad N, Su M, Lou JS, Huang J, Jordan KD, Eng ET, Meyerson JR, Hite RK, Huang XY. Structural basis and mechanism of activation of two different families of G proteins by the same GPCR. Nat Struct Mol Biol. 2021 Nov;28(11):936-944. PMID:34759376 doi:10.1038/s41594-021-00679-2
