Granzin Joachim, Eckhoff Andreas, Weiergräber Oliver H
Institute of Neurosciences and Biophysics, Molecular Biophysics, Research Centre Jülich, D-52425 Jülich, Germany.
J Mol Biol. 2006 Dec 8;364(4):799-809. doi: 10.1016/j.jmb.2006.09.052. Epub 2006 Sep 26.
FKBP42 is a membrane-anchored immunophilin playing a critical role in morphogenesis and development of higher plants. We present the X-ray structure of the cytoplasmic portion of FKBP42 comprising both the FKBP-like domain and the TPR domain at 2.85 A resolution. The data shed light on the probable binding modes of key interaction partners, including HSP90 and two classes of ABC transporters. The resulting models provide a structural background for further investigation of the unique biological properties of this protein.
FKBP42是一种膜锚定亲免蛋白，在高等植物的形态发生和发育中起关键作用。我们展示了FKBP42细胞质部分的X射线结构，其包括FKBP样结构域和TPR结构域，分辨率为2.85埃。这些数据揭示了关键相互作用伙伴（包括HSP90和两类ABC转运蛋白）可能的结合模式。所得模型为进一步研究该蛋白独特的生物学特性提供了结构背景。
