Benke D, Marti T, Heckendorn R, Rehm H, Künzi R, Allgeier H, Angst C, Mohler H
Institute of Pharmacology, University of Zurich, Switzerland.
Eur J Pharmacol. 1993 Jul 15;246(2):179-80. doi: 10.1016/0922-4106(93)90096-r.
The structure of NMDA receptors in situ has been probed with the novel photoaffinity ligand 125I-CGP 55802A. By covalently linking the radioactive high-affinity photolabel to NMDA receptors in bovine brain we have identified a protein of 175 kDa associated with the binding site for NMDA receptor agonists and competitive antagonists. Based on its molecular size the photolabeled protein is likely to correspond to the NR2A and/or NR2B subunit. The photoaffinity ligand will permit the assessment of regulatory changes in NMDA receptor subunit expression.
利用新型光亲和配体125I-CGP 55802A对原位NMDA受体的结构进行了探索。通过将放射性高亲和力光标记与牛脑NMDA受体共价连接，我们鉴定出一种与NMDA受体激动剂和竞争性拮抗剂结合位点相关的175 kDa蛋白质。根据其分子大小，光标记蛋白可能对应于NR2A和/或NR2B亚基。这种光亲和配体将有助于评估NMDA受体亚基表达的调节变化。
