Thielmann Yvonne, Weiergräber Oliver H, Mohrlüder Jeannine, Willbold Dieter
Institut für Neurowissenschaften und Biophysik, Molekulare Biophysik, Forschungszentrum Jülich, Germany.
FEBS J. 2009 Feb;276(4):1140-52. doi: 10.1111/j.1742-4658.2008.06857.x. Epub 2009 Jan 16.
The 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.
γ-氨基丁酸A型受体相关蛋白（GABARAP）是一种多功能衔接蛋白，在细胞内囊泡运输中发挥重要作用，尤其是在神经元细胞中。我们使用光谱学和晶体学技术研究了GABARAP与钙网蛋白相互作用的结构决定因素。具体而言，我们展示了GABARAP与其伴侣蛋白上主要结合表位形成复合物的晶体结构。包含全长钙网蛋白的复合物的分子模型表明了一种新的底物相互作用模式，这可能对钙网蛋白/钙连蛋白家族总体上具有功能意义。
