钙结合蛋白D28K与Ran结合蛋白M相互作用：通过核磁共振光谱法鉴定相互作用结构域。
Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.
作者信息
Lutz Ward, Frank Elena M, Craig Theodore A, Thompson Richele, Venters Ronald A, Kojetin Doug, Cavanagh John, Kumar Rajiv
机构信息
Department of Biochemistry, Research Center, Mayo Clinic and Foundation, 200 First Street SW, Rochester, MN 55905, USA.
出版信息
Biochem Biophys Res Commun. 2003 Apr 18;303(4):1186-92. doi: 10.1016/s0006-291x(03)00499-6.
Calbindin D(28K) is an EF-hand containing protein that plays a vital role in neurological function. We now show that calcium-loaded calbindin D(28K) interacts with Ran-binding protein M, a protein known to play a role in microtubule function. Using NMR methods, we show that a peptide, LASIKNR, derived from Ran-binding protein M, interacts with several regions of the calcium-loaded protein including the amino terminus and two other regions that exhibit conformational exchange on the NMR timescale. We suggest that the interaction between calbindin D(28K) and Ran-binding protein M may be important in calbindin D(28K) function.
钙结合蛋白D（28K）是一种含有EF手结构的蛋白质，在神经功能中起着至关重要的作用。我们现在发现，负载钙的钙结合蛋白D（28K）与Ran结合蛋白M相互作用，Ran结合蛋白M是一种已知在微管功能中起作用的蛋白质。使用核磁共振方法，我们发现来自Ran结合蛋白M的一段肽LASIKNR与负载钙的蛋白质的几个区域相互作用，包括氨基末端以及在核磁共振时间尺度上表现出构象交换的其他两个区域。我们认为钙结合蛋白D（28K）与Ran结合蛋白M之间的相互作用可能对钙结合蛋白D（28K）的功能很重要。
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