Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2187297 | Journal of Molecular Biology | 2008 | 12 Pages |
Abstract
The γ-aminobutyric acid type A (GABAA) 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 GABAA receptor-associated protein complexed with a high-affinity synthetic peptide at 1.3 Å resolution. The data shed light on the probable binding modes of key interaction partners, including the GABAA receptor and the cysteine protease Atg4. The resulting models provide a structural background for further investigation of the unique biological properties of this protein.
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Authors
Oliver H. Weiergräber, Thomas Stangler, Yvonne Thielmann, Jeannine Mohrlüder, Katja Wiesehan, Dieter Willbold,