烟碱型乙酰胆碱受体的配体结合结构域。免疫学分析。
The ligand binding domain of the nicotinic acetylcholine receptor. Immunological analysis.
作者信息
Kachalsky S G, Aladjem M, Barchan D, Fuchs S
机构信息
Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.
出版信息
FEBS Lett. 1993 Mar 8;318(3):264-8. doi: 10.1016/0014-5793(93)80525-y.
The interaction of the acetylcholine receptor (AChR) binding site domain with specific antibodies and with alpha-bungarotoxin (alpha-BTX) has been compared. The cloned and expressed ligand binding domain of the mouse AChR alpha-subunit binds alpha-BTX, whereas the mongoose-expressed domain is not recognized by alpha-BTX. On the other hand, both the mouse and mongoose domains bind to the site-specific monoclonal antibody 5.5. These results demonstrate that the structural requirements for binding of alpha-BTX and mcAb 5.5, both of which interact with the AChR binding site, are distinct from each other.
已对乙酰胆碱受体（AChR）结合位点结构域与特异性抗体及α-银环蛇毒素（α-BTX）的相互作用进行了比较。小鼠AChRα亚基的克隆和表达的配体结合结构域可结合α-BTX，而猫鼬表达的结构域则不被α-BTX识别。另一方面，小鼠和猫鼬的结构域均与位点特异性单克隆抗体5.5结合。这些结果表明，与AChR结合位点相互作用的α-BTX和单克隆抗体5.5的结合结构要求彼此不同。
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