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000014601 0247_ $$2DOI$$a10.1016/j.febslet.2010.12.042
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000014601 041__ $$aeng
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000014601 084__ $$2WoS$$aBiochemistry & Molecular Biology
000014601 084__ $$2WoS$$aBiophysics
000014601 084__ $$2WoS$$aCell Biology
000014601 1001_ $$0P:(DE-HGF)0$$aSeebahn, A.$$b0
000014601 245__ $$aStructural characterization of intracellular C-terminal domains of group III metabotropic glutamate receptors
000014601 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2011
000014601 300__ $$a511 - 516
000014601 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000014601 440_0 $$02052$$aFEBS Letters$$v585$$x0014-5793$$y3
000014601 500__ $$3POF3_Assignment on 2016-02-29
000014601 500__ $$aWe thank Wei Xiang for help with mass spectrometry and Dieter Willbold for helpful discussions. This work was supported by the Deutsche Forschungsgemeinschaft [EN349/5-2, EU-HEALTH-F4-2008-202088, SFB539, SFB796].
000014601 520__ $$aMetabotropic 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.
000014601 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000014601 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000014601 536__ $$0G:(EU-Grant)202088$$aNEUROCYPRES - Neurotransmitter Cys-loop receptors: structure, function and disease (202088)$$c202088$$fFP7-HEALTH-2007-A$$x2
000014601 588__ $$aDataset connected to Web of Science, Pubmed
000014601 65320 $$2Author$$aG-protein coupled receptor
000014601 65320 $$2Author$$aMetabotropic glutamate receptor
000014601 65320 $$2Author$$aNeurotransmitter receptor
000014601 65320 $$2Author$$aShort linear motif
000014601 650_2 $$2MeSH$$aAmino Acid Motifs
000014601 650_2 $$2MeSH$$aAnimals
000014601 650_2 $$2MeSH$$aCircular Dichroism
000014601 650_2 $$2MeSH$$aComputational Biology: methods
000014601 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000014601 650_2 $$2MeSH$$aPeptide Fragments: chemistry
000014601 650_2 $$2MeSH$$aPeptide Fragments: metabolism
000014601 650_2 $$2MeSH$$aProtein Folding
000014601 650_2 $$2MeSH$$aProtein Hydrolysates: chemistry
000014601 650_2 $$2MeSH$$aProtein Interaction Domains and Motifs
000014601 650_2 $$2MeSH$$aProtein Isoforms: chemistry
000014601 650_2 $$2MeSH$$aProtein Isoforms: metabolism
000014601 650_2 $$2MeSH$$aProtein Structure, Secondary
000014601 650_2 $$2MeSH$$aRats
000014601 650_2 $$2MeSH$$aReceptors, Metabotropic Glutamate: chemistry
000014601 650_2 $$2MeSH$$aReceptors, Metabotropic Glutamate: genetics
000014601 650_2 $$2MeSH$$aReceptors, Metabotropic Glutamate: metabolism
000014601 650_2 $$2MeSH$$aRecombinant Fusion Proteins: chemistry
000014601 650_2 $$2MeSH$$aRecombinant Fusion Proteins: metabolism
000014601 650_2 $$2MeSH$$aSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
000014601 650_7 $$00$$2NLM Chemicals$$aPeptide Fragments
000014601 650_7 $$00$$2NLM Chemicals$$aProtein Hydrolysates
000014601 650_7 $$00$$2NLM Chemicals$$aProtein Isoforms
000014601 650_7 $$00$$2NLM Chemicals$$aReceptors, Metabotropic Glutamate
000014601 650_7 $$00$$2NLM Chemicals$$aRecombinant Fusion Proteins
000014601 650_7 $$00$$2NLM Chemicals$$ametabotropic glutamate receptor 6
000014601 650_7 $$00$$2NLM Chemicals$$ametabotropic glutamate receptor 7
000014601 650_7 $$00$$2NLM Chemicals$$ametabotropic glutamate receptor 8
000014601 650_7 $$2WoSType$$aJ
000014601 7001_ $$0P:(DE-HGF)0$$aDinkel, H.$$b1
000014601 7001_ $$0P:(DE-Juel1)132012$$aMohrlüder, J.$$b2$$uFZJ
000014601 7001_ $$0P:(DE-Juel1)VDB57647$$aHartmann, R.$$b3$$uFZJ
000014601 7001_ $$0P:(DE-HGF)0$$aVogel, N.$$b4
000014601 7001_ $$0P:(DE-HGF)0$$aBecker, C.M.$$b5
000014601 7001_ $$0P:(DE-HGF)0$$aSticht, H.$$b6
000014601 7001_ $$0P:(DE-HGF)0$$aEnz, R.$$b7
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000014601 8567_ $$uhttp://dx.doi.org/10.1016/j.febslet.2010.12.042
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