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 inFEBS letters Vol. 318; no. 3; pp. 264 - 268
Main Authors Kachalsky, Sylvia G., Aladjem, Mirit, Barchan, Dora, Fuchs, Sara
Format Journal Article
LanguageEnglish
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.
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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CitedBy_id crossref_primary_10_1016_S0028_3908_99_00116_1
crossref_primary_10_1056_NEJM199406233302507
crossref_primary_10_1016_S0197_0186_99_00154_0
crossref_primary_10_1093_oxfordjournals_molbev_a003967
crossref_primary_10_1016_S0301_4622_00_00114_9
crossref_primary_10_3109_10409239609106586
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Copyright FEBS Letters 318 (1993) 1873-3468 © 2015 Federation of European Biochemical Societies
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Snippet The interaction of the acetylcholine receptor (AChR) binding site domain with specific antibodies and with α‐bungarotoxin (α‐BTX) has been compared. The cloned...
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SourceType Publisher
StartPage 264
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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