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J. Biol. Chem., Vol. 277, Issue 16, 13363-13366, April 19, 2002

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ACCELERATED PUBLICATION
Solution Structure of Human GABA_A Receptor-associated Protein GABARAP
IMPLICATIONS FOR BIOLOGICAL FUNCTION AND ITS REGULATION^*

Thomas Stangler^§, Lorenz M. Mayr^¶, and Dieter Willbold^§**

From the  Institut für Molekulare Biotechnologie, Beutenbergstr. 11, 07745 Jena, Germany, the ^§ Institut für Physikalische Biologie, Heinrich-Heine-Universität, 40225 Düsseldorf, Germany, ^¶ Novartis Pharma AG, CH-4002 Basel, Switzerland, and  Forschungszentrum Jülich, IBI-2, 52425 Jülich, Germany

Control of neurotransmitter receptor expression and delivery to the postsynaptic membrane is of critical importance for neural signal transduction at synapses. The -aminobutyric acid, type A (GABA_A) receptor-associated protein GABARAP was reported to have an important role for movement and sorting of GABA_A receptor molecules to the postsynaptic membrane. GABARAP not only binds to GABA_A receptor 2-subunit but also to tubulin, gephyrin, and ULK1. We present for the first time the high resolution structure of human GABARAP determined by nuclear magnetic resonance in aqueous solution. One part of the molecule, despite being well ordered and rigid on a MHz time scale, exists in at least two different conformations that interchange with each other on a time scale slower than 25 Hz. An important feature of the solution structure is the observation that amino- and carboxyl-terminal ends of the protein directly interact with each other, which is not seen in recently reported crystal structures. The possible biological relevance of these observations for the regulation of GABARAP interactions and functions is discussed.

The atomic coordinates and the structure factors (code 1KOT) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

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