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000005170 0247_ $$2DOI$$a10.1111/j.1742-4658.2008.06857.x
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000005170 041__ $$aeng
000005170 082__ $$a540
000005170 084__ $$2WoS$$aBiochemistry & Molecular Biology
000005170 1001_ $$0P:(DE-Juel1)VDB77156$$aThielmann, Y.$$b0$$uFZJ
000005170 245__ $$aStructural framework of the GABARAP-calreticulin interface - implications for substrate binding to endoplasmic reticulum chaperones
000005170 260__ $$aOxford [u.a.]$$bWiley-Blackwell$$c2009
000005170 300__ $$a1140 - 1152
000005170 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000005170 3367_ $$2DRIVER$$aarticle
000005170 440_0 $$017341$$aFEBS Journal$$v276$$x1742-464X$$y4
000005170 500__ $$aThe authors wish to thank Olga Dietz for excellent technical assistance. O. H. WeiergrAber is grateful to Georg Buldt for continuous generous support. Moreover, assistance by the ESRF staff at beamline ID14-1 is acknowledged. This study was supported by a research grant from the Deutsche Forschungsgemeinschaft (DFG) to D. Willbold (Wi1472/5).
000005170 520__ $$aThe 4-aminobutyrate type A receptor-associated protein (GABARAP) is a versatile adaptor protein that plays an important role in intracellular vesicle trafficking, particularly in neuronal cells. We have investigated the structural determinants underlying the interaction of GABARAP with calreticulin using spectroscopic and crystallographic techniques. Specifically, we present the crystal structure of GABARAP in complex with its major binding epitope on the chaperone. Molecular modeling of a complex containing full-length calreticulin suggests a novel mode of substrate interaction, which may have functional implications for the calreticulin/calnexin family in general.
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000005170 65320 $$2Author$$a4-aminobutyrate type A receptor-associated protein (GABARAP)
000005170 65320 $$2Author$$acalreticulin
000005170 65320 $$2Author$$aprotein-protein interaction
000005170 65320 $$2Author$$astructure model
000005170 65320 $$2Author$$aX-ray crystallography
000005170 650_2 $$2MeSH$$aAdaptor Proteins, Signal Transducing: chemistry
000005170 650_2 $$2MeSH$$aAdaptor Proteins, Signal Transducing: metabolism
000005170 650_2 $$2MeSH$$aCalreticulin: chemistry
000005170 650_2 $$2MeSH$$aCalreticulin: metabolism
000005170 650_2 $$2MeSH$$aEndoplasmic Reticulum: metabolism
000005170 650_2 $$2MeSH$$aHumans
000005170 650_2 $$2MeSH$$aMicrotubule-Associated Proteins: chemistry
000005170 650_2 $$2MeSH$$aMicrotubule-Associated Proteins: metabolism
000005170 650_2 $$2MeSH$$aModels, Molecular
000005170 650_2 $$2MeSH$$aMolecular Chaperones: chemistry
000005170 650_2 $$2MeSH$$aMolecular Chaperones: metabolism
000005170 650_2 $$2MeSH$$aProtein Binding
000005170 650_2 $$2MeSH$$aSubstrate Specificity
000005170 650_7 $$00$$2NLM Chemicals$$aAdaptor Proteins, Signal Transducing
000005170 650_7 $$00$$2NLM Chemicals$$aCalreticulin
000005170 650_7 $$00$$2NLM Chemicals$$aGABARAP protein, human
000005170 650_7 $$00$$2NLM Chemicals$$aMicrotubule-Associated Proteins
000005170 650_7 $$00$$2NLM Chemicals$$aMolecular Chaperones
000005170 650_7 $$2WoSType$$aJ
000005170 7001_ $$0P:(DE-Juel1)131988$$aWeiergräber, O.H.$$b1$$uFZJ
000005170 7001_ $$0P:(DE-Juel1)132012$$aMohrlüder, J.$$b2$$uFZJ
000005170 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b3$$uFZJ
000005170 773__ $$0PERI:(DE-600)2172518-4$$a10.1111/j.1742-4658.2008.06857.x$$gVol. 276, p. 1140 - 1152$$p1140 - 1152$$q276<1140 - 1152$$tThe @FEBS journal$$v276$$x1742-464X$$y2009
000005170 8567_ $$uhttp://dx.doi.org/10.1111/j.1742-4658.2008.06857.x
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