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Structural characterization of intracellular C‐terminal domains of group III metabotropic glutamate receptors
Author(s) -
Seebahn Angela,
Dinkel Holger,
Mohrlüder Jeannine,
Hartmann Rudolf,
Vogel Nico,
Becker Cord-Michael,
Sticht Heinrich,
Enz Ralf
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.12.042
Subject(s) - metabotropic glutamate receptor , chemistry , metabotropic glutamate receptor 2 , metabotropic glutamate receptor 1 , circular dichroism , class c gpcr , biophysics , glutamate receptor , biochemistry , stereochemistry , receptor , biology
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.