FEBS Letters · 2011 · 13 citations · 12 references
Life SciencesBiochemistryNeuroscienceMolecular NeurobiologyMolecular NeuroscienceStructural BiologyGlobular ProteinsGlutamatergic SignalingLigand BindingNeurotransmitter ReceptorsProtein StructureReceptor-ligand InteractionsCircular DichroismCircular Dichroism AnalysisConformational Changes In ReceptorsIntracellular DomainsMetabotropic ReceptorsReceptor Conformational RegulationReceptor-ligand Structural BiologyShort Linear Motifs
Metabotropic glutamate receptors (mGluRs) are regulated by interacting proteins that mostly bind to their intracellular C-termini. Here, we investigated if mGluR6, mGluR7a and mGluR8a C-termini form predefined binding surfaces or if they were rather unstructured. Limited tryptic digest of purified peptides argued against the formation of stable globular folds. Circular dichroism, (1)H NMR and (1)H(15)N HSQC spectra indicated the absence of rigid secondary structure elements. Furthermore, we localized short linear binding motifs in the unstructured receptor domains. Our data provide evidence that protein interactions of the analyzed mGluR C-termini are mediated rather by short linear motifs than by preformed folds.
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Crystal structure of the human β2 adrenergic G-protein-coupled receptor
Søren G. F. Rasmussen, Hee‐Jung Choi, Daniel M. Rosenbaum et al. · Nature · 2007 · 1.9K citations