scholarly journals Expansion of Secretin-Like G Protein-Coupled Receptors and Their Peptide Ligands via Local Duplications Before and After Two Rounds of Whole-Genome Duplication

2013 ◽  
Vol 30 (5) ◽  
pp. 1119-1130 ◽  
Author(s):  
Jong-Ik Hwang ◽  
Mi Jin Moon ◽  
Sumi Park ◽  
Dong-Kyu Kim ◽  
Eun Bee Cho ◽  
...  
Keyword(s):  
G Protein ◽  
Whole Genome Duplication ◽  
Genome Duplication ◽  
G Protein Coupled Receptors ◽  
Peptide Ligands ◽  
Whole Genome ◽  
Before And After ◽  
G Protein Coupled

Mass-spectrometry-based method for screening of new peptide ligands for G-protein-coupled receptors

2015 ◽  
Vol 407 (18) ◽  
pp. 5299-5307 ◽  
Author(s):  
Camila T. Cologna ◽  
Nicolas Gilles ◽  
Julien Echterbille ◽  
Michel Degueldre ◽  
Denis Servent ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
G Protein ◽  
G Protein Coupled Receptors ◽  
Peptide Ligands ◽  
G Protein Coupled

scholarly journals Whole-Genome Analysis of 60 G Protein-Coupled Receptors in Caenorhabditis elegans by Gene Knockout with RNAi

2003 ◽  
Vol 13 (19) ◽  
pp. 1715-1720 ◽  
Author(s):  
Christopher D. Keating ◽  
Neline Kriek ◽  
Margaret Daniels ◽  
Neville R. Ashcroft ◽  
Neil A. Hopper ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
G Protein ◽  
Genome Analysis ◽  
Gene Knockout ◽  
G Protein Coupled Receptors ◽  
Whole Genome ◽  
Whole Genome Analysis ◽  
G Protein Coupled

scholarly journals Molecular Basis of Secretin Docking to Its Intact Receptor Using Multiple Photolabile Probes Distributed throughout the Pharmacophore

2011 ◽  
Vol 286 (27) ◽  
pp. 23888-23899 ◽  
Author(s):  
Maoqing Dong ◽  
Polo C.-H. Lam ◽  
Delia I. Pinon ◽  
Keiko Hosohata ◽  
Andrew Orry ◽  
...  
Keyword(s):  
G Protein ◽  
Molecular Basis ◽  
Peptide Mapping ◽  
G Protein Coupled Receptors ◽  
Peptide Ligands ◽  
Amino Terminus ◽  
Amino Terminal ◽  
Binding Cleft ◽  
Mutant Receptors ◽  
G Protein Coupled

The molecular basis of ligand binding and activation of family B G protein-coupled receptors is not yet clear due to the lack of insight into the structure of intact receptors. Although NMR and crystal structures of amino-terminal domains of several family members support consistency in general structural motifs that include a peptide-binding cleft, there are variations in the details of docking of the carboxyl terminus of peptide ligands within this cleft, and there is no information about siting of the amino terminus of these peptides. There are also no empirical data to orient the receptor amino terminus relative to the core helical bundle domain. Here, we prepared a series of five new probes, incorporating photolabile moieties into positions 2, 15, 20, 24, and 25 of full agonist secretin analogues. Each bound specifically to the receptor and covalently labeled single distinct receptor residues. Peptide mapping of labeled wild-type and mutant receptors identified that the position 15, 20, and 25 probes labeled residues within the distal amino terminus of the receptor, whereas the position 24 probe labeled the amino terminus adjacent to TM1. Of note, the position 2 probe labeled a residue within the first extracellular loop of the receptor, a region not previously labeled, providing an important new constraint for docking the amino-terminal region of secretin to its receptor core. These additional experimentally derived constraints help to refine our understanding of the structure of the secretin-intact receptor complex and provide new insights into understanding the molecular mechanism for activation of family B G protein-coupled receptors.

scholarly journals Evolution of the shut-off steps of vertebrate phototransduction

Open Biology ◽  
2018 ◽  
Vol 8 (1) ◽  
pp. 170232 ◽  
Author(s):  
Trevor D. Lamb ◽  
Hardip R. Patel ◽  
Aaron Chuah ◽  
David M. Hunt
Keyword(s):  
G Protein ◽  
Whole Genome Duplication ◽  
Genome Duplication ◽  
Parallel Evolution ◽  
Whole Genome ◽  
Gene Expansion ◽  
Protein Receptor ◽  
Receptor Kinases ◽  
Rod And Cone Photoreceptors ◽  
Ancestral Vertebrate

Different isoforms of the genes involved in phototransduction are expressed in vertebrate rod and cone photoreceptors, providing a unique example of parallel evolution via gene duplication. In this study, we determine the molecular phylogeny of the proteins underlying the shut-off steps of phototransduction in the agnathan and jawed vertebrate lineages. For the G-protein receptor kinases (GRKs), the GRK1 and GRK7 divisions arose prior to the divergence of tunicates, with further expansion during the two rounds of whole-genome duplication (2R); subsequently, jawed and agnathan vertebrates retained different subsets of three isoforms of GRK. For the arrestins, gene expansion occurred during 2R. Importantly, both for GRKs and arrestins, the respective rod isoforms did not emerge until the second round of 2R, just prior to the separation of jawed and agnathan vertebrates. For the triplet of proteins mediating shut-off of the G-protein transducin, RGS9 diverged from RGS11, probably at the second round of 2R, whereas Gβ5 and R9AP appear not to have undergone 2R expansion. Overall, our analysis provides a description of the duplications and losses of phototransduction shut-off genes that occurred during the transition from a chordate with only cone-like photoreceptors to an ancestral vertebrate with both cone- and rod-like photoreceptors.

scholarly journals Cell‐free synthesis of isotopically labelled peptide ligands for the functional characterization of G protein‐coupled receptors

FEBS Open Bio ◽  
2015 ◽  
Vol 6 (1) ◽  
pp. 90-102 ◽  
Author(s):  
Lisa Joedicke ◽  
Raphael Trenker ◽  
Julian D. Langer ◽  
Hartmut Michel ◽  
Julia Preu
Keyword(s):  
G Protein ◽  
Functional Characterization ◽  
G Protein Coupled Receptors ◽  
Peptide Ligands ◽  
G Protein Coupled

NMR studies of CCK-8/CCK1 complex support membrane-associated pathway for ligand-receptor interaction

2002 ◽  
Vol 80 (5) ◽  
pp. 383-387 ◽  
Author(s):  
Craig Giragossian ◽  
Maria Pellegrini ◽  
Dale F Mierke
Keyword(s):  
G Protein ◽  
Structural Features ◽  
G Protein Coupled Receptors ◽  
Peptide Ligands ◽  
Receptor Interaction ◽  
Peptide Ligand ◽  
Receptor Subtype ◽  
Nmr Studies ◽  
Receptor Complexes ◽  
G Protein Coupled

The interaction of peptide ligands with their associated G-protein-coupled receptors has been examined by a number of different experimental approaches over the years. We have been developing an approach utilizing high-resolution NMR to determine the structural features of the peptide ligand, well-designed fragments of the receptor, and the ligand–receptor complexes formed upon titration of the peptide hormone. The results from these investigations provide evidence for a membrane-associated pathway for the initial interaction of peptide ligands with the receptor. Here, our results from the investigation of the interaction of CCK-8 with the CCK1 receptor are described. Our spectroscopic results clearly show that both CCK-8 and the regions of CCK1 with which it interacts are closely associated with the zwitterionic interface of the lipids utilized in our solution spectroscopic studies.Key words: G-protein-coupled receptors, NMR structural characterization, cholecystokinin, CCK-8, cholecystokinin receptor, subtype 1, CCK1, peptide hormones.

Triblock peptide–linker–lipid molecular design improves potency of peptide ligands targeting family B G protein-coupled receptors

2015 ◽  
Vol 51 (28) ◽  
pp. 6157-6160 ◽  
Author(s):  
Yuting Liu ◽  
Yingying Cai ◽  
Wei Liu ◽  
Xiao-Han Li ◽  
Elizabeth Rhoades ◽  
...  
Keyword(s):  
G Protein ◽  
Molecular Design ◽  
G Protein Coupled Receptors ◽  
Peptide Ligands ◽  
G Protein Coupled

Design and characterization of triblock peptide–linker–lipid constructs for targeting family B G protein-couple receptors with improved bioactivity and biostability.

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