Wang Yuning, Tadayon Roya, Shaw Gary S
Department of Biochemistry, The University of Western Ontario, London, ON, Canada.
Methods Mol Biol. 2019;1929:311-324. doi: 10.1007/978-1-4939-9030-6_20.
S100B is a dimeric EF-hand protein that undergoes a calcium-induced conformational change and interacts with a wide range of proteins to modulate their functions. The dopamine D2 receptor is one potential S100B binding partner that may play a key role in neurological processing. In this chapter, we describe the use of NMR spectroscopy to examine the interaction between calcium-bound S100B and the third intracellular loop (IC3) from the dopamine D2 receptor. We provide details that allow the strength of the interaction (K ) between the two proteins to be determined and the IC3 site of interaction on the structure of S100B to be identified. Both these characteristics can be identified from a single series of nondestructive experiments.
S100B是一种二聚体EF手型蛋白，会经历钙诱导的构象变化，并与多种蛋白质相互作用以调节其功能。多巴胺D2受体是一个潜在的S100B结合伴侣，可能在神经加工过程中起关键作用。在本章中，我们描述了使用核磁共振光谱法来研究钙结合的S100B与多巴胺D2受体的第三个细胞内环（IC3）之间的相互作用。我们提供了详细信息，以便确定两种蛋白质之间相互作用的强度（K），并确定S100B结构上的IC3相互作用位点。这两个特征都可以从一系列无损实验中识别出来。
