Structural characterization of intracellular C-terminal domains of group III metabotropic glutamate receptors |
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Authors: | Seebahn Angela Dinkel Holger Mohrlüder Jeannine Hartmann Rudolf Vogel Nico Becker Cord-Michael Sticht Heinrich Enz Ralf |
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Institution: | aInstitut für Biochemie (Emil-Fischer-Zentrum), Friedrich-Alexander-Universität Erlangen-Nürnberg, 91045 Erlangen, Germany;bInstitut für Strukturbiologie und Biophysik 3 (Strukturbiochemie), Forschungszentrum Jülich, 52425 Jülich, Germany |
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Abstract: | 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, 1H NMR and 1H15N 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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Keywords: | G-protein coupled receptor Metabotropic glutamate receptor Neurotransmitter receptor Short linear motif |
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