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3.0 A crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation
This work suggests that RAMP2 (Montrer RAMP2 Kits ELISA) may modify the agonist activity and trafficking of the GCGR, with potential relevance to production of new peptide analogs with selective agonist activities.
Data suggest that GCGR activation proceeds via a mechanism in which transmembrane helix 6 (TM6) is held in an inactive conformation by a conserved polar core and a hydrophobic lock (involving intracellular loop 3, IC3); mutations in the corresponding polar core of GCGR disrupt these inhibitory elements, allow TM6 to swing outward, and induce constitutive G protein signaling.
The activation of the GCGR is characterized by the outward movement of the intracellular side of helix VI. In the active state of the GCGR, the Arg173(2.46)-Ser350(6.41) and Glu245(3.50)-Thr351(6.42) hydrogen bonds break, and the chi1 rotamer of Phe322(5.54) changes from perpendicular to parallel to helix VI.
In the glucagon receptor (GCGR) and glucagon-like peptide-1 receptor (GLP-1R (Montrer GLP1R Kits ELISA)), the extracellular domain is required for signaling even when the hormone is covalently linked to the transmembrane domain.
2.5 A crystal structure of human GCGR in complex with the antagonist MK-0893, which is found to bind to an allosteric site outside the seven transmembrane helical bundle in a position between TM6 and TM7 extending into the lipid bilayer
Molecular dynamics and disulfide crosslinking studies suggest that apo (Montrer C9orf3 Kits ELISA)-GCGR can adopt both an open and closed conformation associated with extensive contacts between the ECD (Montrer SHFM1 Kits ELISA) and 7TM domain. Glucagon (Montrer GCG Kits ELISA) binds to GCGR by a conformational selection mechanism.
glucagon (Montrer GCG Kits ELISA) cell adenomatosis with GCGR germline mutations seems to follow an autosomal-recessive trait.
Using a real-time time-resolved FRET-based internalization assay, we show that GLP-1R (Montrer GLP1R Kits ELISA), GIPR (Montrer GIPR Kits ELISA), and GCGR internalize with differential properties
crystal structure of the seven transmembrane helical domain of human GCGR at 3.4 A resolution, and a hybrid model of glucagon (Montrer GCG Kits ELISA) bound to GCGR to understand the molecular recognition of the receptor for its native ligand
GcgR knockout (Gcgr(-/-)) mice displayed lower blood glucose levels accompanied by elevated plasma ghrelin (Montrer GHRL Kits ELISA) levels. Hyperglycemia was averted in streptozocin treated Gcgr(-/-) mice and the plasma ghrelin (Montrer GHRL Kits ELISA) level was further increased.
glucagon receptor antagonist improves glycemia in diet-induced obese angptl4 (Montrer ANGPTL4 Kits ELISA) knockout mice without increasing glucagon (Montrer GCG Kits ELISA) levels or alpha-cell proliferation, underscoring the importance of this protein.
Data indicate that the exocrine pancreas in the glucagon receptor Gcgr-/- mice exhibited larger nuclear size than in WT or heterozygous controls, most obviously at old ages.
Simultaneous and sufficient activation of GLP1R (Montrer GLP1R Kits ELISA) is required to reduce GCCR (Montrer NR3C1 Kits ELISA) mediated blood glucose elevation following administration of a GLP1R (Montrer GLP1R Kits ELISA)/GCGR co-agonist.
Knockdown of liver glucagon receptor in mice reduces blood glucose and increases blood LDL levels.
Gcgr(-/-) mice became lethargic (Montrer CACNB4 Kits ELISA) & cachexic & died early. Autopsy revealed numerous PNETs up to 15 mm in diameter in most well-preserved Gcgr(-/-) pancreata.
Data suggest that GcgR activation raises hepatic expression of fibroblast growth factor 21 (FGF21 (Montrer FGF21 Kits ELISA)) and increases circulating levels of FGF21 (Montrer FGF21 Kits ELISA); GcgR activation induces body weight loss and stimulates lipid metabolism.
These results suggest that a circulating factor generated after disruption of hepatic Gcgr signaling can increase alpha-cell proliferation independent of direct pancreatic input.
GRA1 is a potent glucagon receptor antagonist with strong antihyperglycemic efficacy in preclinical models and prominent effects on hepatic gene-expression related to amino acid metabolism
Data suggest that both Gcgr activity and glucagon-like peptide 1 (Montrer GCG Kits ELISA)/Glp1r (Montrer GLP1R Kits ELISA) signal transduction in central nervous system are involved in control of interscapular brown adipose tissue thermogenesis.
The protein encoded by this gene is a glucagon receptor that is important in controlling blood glucose levels. Defects in this gene are a cause of non-insulin-dependent diabetes mellitus (NIDDM).
, glucagon receptor-like
, glucagon receptor perhaps same as Niddm3