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000000344 0247_ $$2DOI$$a10.1016/j.jmb.2008.06.086
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000000344 084__ $$2WoS$$aBiochemistry & Molecular Biology
000000344 1001_ $$0P:(DE-Juel1)131988$$aWeiergräber, O. H.$$b0$$uFZJ
000000344 245__ $$aLigand binding mode of GABA(A) receptor-associated protein
000000344 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2008
000000344 300__ $$a1320 - 1331
000000344 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000000344 440_0 $$03552$$aJournal of Molecular Biology$$v381$$x0022-2836
000000344 500__ $$aThe authors wish to thank Joachim Granzin for helpful discussion and Olga Dietz for excellent technical assistance. O.H.W. is grateful to Georg Buldt for continuous generous support. Moreover, assistance by the ESRF staff at beamline ID14-1 is acknowledged. This study was supported by a research grant from the Deutsche Forschungsgemeinschaft to D.W. (Wi1472/5).
000000344 520__ $$aThe gamma-aminobutyric acid type A (GABA(A)) receptor-associated protein is a versatile adaptor protein playing an important role in intracellular vesicle trafficking, particularly in neuronal cells. We present the X-ray structure of the soluble form of human GABA(A) receptor-associated protein complexed with a high-affinity synthetic peptide at 1.3 A resolution. The data shed light on the probable binding modes of key interaction partners, including the GABA(A) receptor and the cysteine protease Atg4. The resulting models provide a structural background for further investigation of the unique biological properties of this protein.
000000344 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
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000000344 65320 $$2Author$$aGABARAP
000000344 65320 $$2Author$$aGABA(A) receptor
000000344 65320 $$2Author$$asynthetic peptide
000000344 65320 $$2Author$$aphage display
000000344 65320 $$2Author$$aX-ray crystallography
000000344 650_2 $$2MeSH$$aAdaptor Proteins, Signal Transducing: chemistry
000000344 650_2 $$2MeSH$$aAdaptor Proteins, Signal Transducing: metabolism
000000344 650_2 $$2MeSH$$aHumans
000000344 650_2 $$2MeSH$$aKinetics
000000344 650_2 $$2MeSH$$aLigands
000000344 650_2 $$2MeSH$$aMagnetic Resonance Spectroscopy
000000344 650_2 $$2MeSH$$aMicrotubule-Associated Proteins: chemistry
000000344 650_2 $$2MeSH$$aMicrotubule-Associated Proteins: metabolism
000000344 650_2 $$2MeSH$$aModels, Molecular
000000344 650_2 $$2MeSH$$aPeptides: metabolism
000000344 650_2 $$2MeSH$$aProtein Binding
000000344 650_2 $$2MeSH$$aProtein Structure, Secondary
000000344 650_2 $$2MeSH$$aSurface Plasmon Resonance
000000344 650_7 $$00$$2NLM Chemicals$$aAdaptor Proteins, Signal Transducing
000000344 650_7 $$00$$2NLM Chemicals$$aGABARAP protein, human
000000344 650_7 $$00$$2NLM Chemicals$$aLigands
000000344 650_7 $$00$$2NLM Chemicals$$aMicrotubule-Associated Proteins
000000344 650_7 $$00$$2NLM Chemicals$$aPeptides
000000344 650_7 $$2WoSType$$aJ
000000344 7001_ $$0P:(DE-Juel1)VDB8627$$aStangler, T.$$b1$$uFZJ
000000344 7001_ $$0P:(DE-Juel1)VDB77156$$aThielmann, Y.$$b2$$uFZJ
000000344 7001_ $$0P:(DE-Juel1)132012$$aMohrlüder, J.$$b3$$uFZJ
000000344 7001_ $$0P:(DE-Juel1)VDB15437$$aWiesehan, K.$$b4$$uFZJ
000000344 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b5$$uFZJ
000000344 773__ $$0PERI:(DE-600)1355192-9$$a10.1016/j.jmb.2008.06.086$$gVol. 381, p. 1320 - 1331$$p1320 - 1331$$q381<1320 - 1331$$tJournal of molecular biology$$v381$$x0022-2836$$y2008
000000344 8567_ $$uhttp://dx.doi.org/10.1016/j.jmb.2008.06.086
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