XRAY DIFFRACTION OF CD45 CRYSTALS

野生型R亚基的三维结构将 提供了关于两种单体如何相对 蛋白质如何二聚化，铰链如何 区域折叠，在缺失突变体中完全无序 结构 该二聚化结构域还提供了一个对接位点， 将全酶锚定在各种支架蛋白上， 细胞质和细胞核。 突变体R亚基的晶体 cAMP结合位点的缺陷。 它们的结构在高处 分辨率对于定义这些分子的分子特征至关重要。 cAMP结合位点和了解构象变化 其由cAMP结合诱导。

The 3-dimensional structure of the wild type R subunit will provide important information on how the two monomers are relatively oriented to each other, how the protein dimerizies and how the hinge region folds, which is totally disordered in the deletion mutant structure. This dimerization domain also provides a docking site for anchoring the holoenzyme to a variety of scaffolding proteins both in cytoplasm and the nucleus. The crystals of mutant R subunits have defects in their cAMP binding sites. Their structures at high resolution are essential for defining the molecular features of these cAMP binding sites and for understanding the conformational changes which are induced by cAMP binding.