The ligand binding domain of the nicotinic acetylcholine receptor
The interaction of the acetylcholine receptor (AChR) binding site domain with specific antibodies and with α‐bungarotoxin (α‐BTX) has been compared. The cloned and expressed ligand binding domain of the mouse AChR α‐subunit binds α‐BTX, whereas the mongoose‐expressed domain is not recognized by α‐BT...
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Published in | FEBS letters Vol. 318; no. 3; pp. 264 - 268 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
08.03.1993
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Abstract | The interaction of the acetylcholine receptor (AChR) binding site domain with specific antibodies and with α‐bungarotoxin (α‐BTX) has been compared. The cloned and expressed ligand binding domain of the mouse AChR α‐subunit binds α‐BTX, whereas the mongoose‐expressed domain is not recognized by α‐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 α‐BTX and mcAb 5.5, both of which interact with the AChR binding site, are distinct from each other. |
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AbstractList | The interaction of the acetylcholine receptor (AChR) binding site domain with specific antibodies and with α‐bungarotoxin (α‐BTX) has been compared. The cloned and expressed ligand binding domain of the mouse AChR α‐subunit binds α‐BTX, whereas the mongoose‐expressed domain is not recognized by α‐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 α‐BTX and mcAb 5.5, both of which interact with the AChR binding site, are distinct from each other. |
Author | Barchan, Dora Aladjem, Mirit Kachalsky, Sylvia G. Fuchs, Sara |
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Copyright | FEBS Letters 318 (1993) 1873-3468 © 2015 Federation of European Biochemical Societies |
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SubjectTerms | Acetylcholine receptor Ligand binding site Monoclonal antibody 5.5 α-Bungarotoxin |
Title | The ligand binding domain of the nicotinic acetylcholine receptor |
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