Structural characterization of intracellular C-terminal domains of group III metabotropic glutamate receptors.

Seebahn A, Dinkel H, Mohrlüder J, Hartmann R, Vogel N, Becker CM, Sticht H, Enz R (2011)

Publication Type: Journal article

Publication year: 2011

Journal

Publisher: Elsevier

Pages Range: 511-516

Journal Issue: 585

DOI: 10.1016/j.febslet.2010.12.042

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 ¹H ¹⁵N 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. © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Authors with CRIS profile

Involved external institutions

European Molecular Biology Laboratory (EMBL) Germany (DE)

How to cite

APA:

Seebahn, A., Dinkel, H., Mohrlüder, J., Hartmann, R., Vogel, N., Becker, C.-M.,... Enz, R. (2011). Structural characterization of intracellular C-terminal domains of group III metabotropic glutamate receptors. Febs Letters, 585, 511-516. https://doi.org/10.1016/j.febslet.2010.12.042

MLA:

Seebahn, Angela, et al. "Structural characterization of intracellular C-terminal domains of group III metabotropic glutamate receptors." Febs Letters 585 (2011): 511-516.

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