Monitoring Interactions Between S100B and the Dopamine D2 Receptor Using NMR Spectroscopy
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 (Kd) 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.
Key wordsS100B Dopamine receptor Protein interactions Binding site Protein structure
This research was supported by a research grant (MOP 93520) from the Canadian Institutes of Health Research (GSS). We thank Brian Dempsey for the helpful discussions. Yuning Wang and Roya Tadayon contributed equally to this work.
- 20.Katzung BG (2001) Introduction to autonomic pharmacology. In: Basic and clinical pharmacology, 8th edn. The McGraw Hill Companies, Inc, New York, NYGoogle Scholar