ArticleProceedings of the National Academy of Sciences of the United States of America2009
Structural and kinetic modeling of an activating helix switch in the rhodopsin-transducin interface.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 51 citations in OpenAlex.
- Mechanistic insights into G-protein coupling with an agonist-bound G-protein-coupled receptor.Nature structural & molecular biology · 2024Article
- Structural aspects of rod opsin and their implication in genetic diseases.Pflugers Archiv : European journal of physiology · 2021Review
- Assembly of a GPCR-G Protein Complex.Cell · 2019Article
- A New Multisystem Disorder Caused by the Gαs Mutation p.F376V.The Journal of clinical endocrinology and metabolism · 2019Article
- Evaluation of variability in high-resolution protein structures by global distance scoring.Heliyon · 2018Article
- In vivo optophysiology reveals that G-protein activation triggers osmotic swelling and increased light scattering of rod photoreceptors.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Functional Role of the C-Terminal Amphipathic Helix 8 of Olfactory Receptors and Other G Protein-Coupled Receptors.International journal of molecular sciences · 2016Review
- SL2: an interactive webtool for modeling of missing segments in proteins.Nucleic acids research · 2016Article
- SIGNAL TRANSDUCTION. Structural basis for nucleotide exchange in heterotrimeric G proteins.Science (New York, N.Y.) · 2015Article
- Role of Structural Dynamics at the Receptor G Protein Interface for Signal Transduction.PloS one · 2015Article
- Energetic analysis of the rhodopsin-G-protein complex links the α5 helix to GDP release.Nature structural & molecular biology · 2014Article
- Novel insights on thyroid-stimulating hormone receptor signal transduction.Endocrine reviews · 2013Review
- Effect of channel mutations on the uptake and release of the retinal ligand in opsin.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Molecular evolution of the neuropeptide S receptor.PloS one · 2012Article
- The cytoplasmic rhodopsin-protein interface: potential for drug discovery.Current drug targets · 2012Review
- From molecular details of the interplay between transmembrane helices of the thyrotropin receptor to general aspects of signal transduction in family a G-protein-coupled receptors (GPCRs).The Journal of biological chemistry · 2011Article
- Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Recognition in the face of diversity: interactions of heterotrimeric G proteins and G protein-coupled receptor (GPCR) kinases with activated GPCRs.The Journal of biological chemistry · 2011Review
- Article
- Principles and determinants of G-protein coupling by the rhodopsin-like thyrotropin receptor.PloS one · 2010Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Extracellular signals prompt G protein-coupled receptors (GPCRs) to adopt an active conformation (R*) and catalyze GDP/GTP exchange in the alpha-subunit of intracellular G proteins (Galphabetagamma). Kinetic analysis of transducin (G(t)alphabetagamma) activation shows that an intermediary R*xG(t)alphabetagamma.GDP complex is formed that precedes GDP release and formation of the nucleotide-free R*xG protein complex. Based on this reaction sequence, we explore the dynamic interface between the proteins during formation of these complexes. We start from the R* conformation stabilized by a G(t)alpha C-terminal peptide (GalphaCT) obtained from crystal structures of the GPCR opsin. Molecular modeling allows reconstruction of the fully elongated C-terminal alpha-helix of G(t)alpha (alpha5) and shows how alpha5 can be docked to the open binding site of R*. Two modes of interaction are found. One of them--termed stable or S-interaction--matches the position of the GalphaCT peptide in the crystal structure and reproduces the hydrogen-bonding networks between the C-terminal reverse turn of GalphaCT and conserved E(D)RY and NPxxY(x)(5,6)F regions of the GPCR. The alternative fit--termed intermediary or I-interaction--is distinguished by a tilt (42 degrees ) and rotation (90 degrees ) of alpha5 relative to the S-interaction and shows different alpha5 contacts with the NPxxY(x)(5,6)F region and the second cytoplasmic loop of R*. From the 2 alpha5 interactions, we derive a "helix switch" mechanism for the transition of R*xG(t)alphabetagamma.GDP to the nucleotide-free R*xG protein complex that illustrates how alpha5 might act as a transmission rod to propagate the conformational change from the receptor-G protein interface to the nucleotide binding site.
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