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000007139 0247_ $$2pmid$$apmid:19462014
000007139 0247_ $$2DOI$$a10.1039/b900425d
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000007139 084__ $$2WoS$$aBiochemistry & Molecular Biology
000007139 1001_ $$0P:(DE-Juel1)VDB77156$$aThielmann, Y.$$b0$$uFZJ
000007139 245__ $$aStructural characterization of GABARAP-ligand interactions
000007139 260__ $$aCambridge$$bRoyal Society of Chemistry$$c2009
000007139 300__ $$a575 - 579
000007139 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000007139 440_0 $$020661$$aMolecular BioSystems$$v5$$x1742-206X
000007139 500__ $$aO.H.W. is grateful to Georg Buldt for continuous generous support. Moreover, assistance by the beamline staff at ESRF (Grenoble, France) is acknowledged. This study was supported by a research grant from the Deutsche Forschungsgemeinschaft to D. W. (Wi1472/5).
000007139 520__ $$aThe GABA(A) receptor-associated protein (GABARAP) plays an important role in intracellular trafficking of several proteins. It undergoes a C-terminal lipidation process that enables anchoring in the cytosolic leaflet of cellular membranes. While the three-dimensional structure of GABARAP itself has been determined, structural investigation of complexes with its interaction partners has just commenced. Studies with indole derivatives revealed that GABARAP features two hydrophobic binding sites (hp1 and hp2). These also play an essential role in complex formation with the native ligand calreticulin. Furthermore, a model of hexameric N-ethylmaleimide-sensitive factor (NSF) suggests that binding of GABARAP to this molecular machine may involve a similar site. Since hp1 and hp2 are highly conserved throughout the GABARAP family, the relevance of the structural data presented here is likely to extend to GABARAP homologues.
000007139 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
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000007139 650_2 $$2MeSH$$aAmino Acid Sequence
000007139 650_2 $$2MeSH$$aAnimals
000007139 650_2 $$2MeSH$$aCalreticulin: chemistry
000007139 650_2 $$2MeSH$$aCalreticulin: metabolism
000007139 650_2 $$2MeSH$$aClathrin Heavy Chains: chemistry
000007139 650_2 $$2MeSH$$aClathrin Heavy Chains: metabolism
000007139 650_2 $$2MeSH$$aHumans
000007139 650_2 $$2MeSH$$aLigands
000007139 650_2 $$2MeSH$$aModels, Molecular
000007139 650_2 $$2MeSH$$aProtein Binding
000007139 650_2 $$2MeSH$$aProtein Structure, Tertiary
000007139 650_2 $$2MeSH$$aReceptors, GABA-A: chemistry
000007139 650_2 $$2MeSH$$aReceptors, GABA-A: metabolism
000007139 650_7 $$00$$2NLM Chemicals$$aCalreticulin
000007139 650_7 $$00$$2NLM Chemicals$$aLigands
000007139 650_7 $$00$$2NLM Chemicals$$aReceptors, GABA-A
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000007139 7001_ $$0P:(DE-Juel1)131988$$aWeiergräber, O.H.$$b1$$uFZJ
000007139 7001_ $$0P:(DE-Juel1)132012$$aMohrlüder, J.$$b2$$uFZJ
000007139 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b3$$uFZJ
000007139 773__ $$0PERI:(DE-600)2188635-0$$a10.1039/b900425d$$gVol. 5, p. 575 - 579$$p575 - 579$$q5<575 - 579$$tMolecular BioSystems$$v5$$x1742-206X$$y2009
000007139 8567_ $$uhttp://dx.doi.org/10.1039/b900425d
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