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The ligand binding domain of the nicotinic acetylcholine receptor
Author(s) -
Kachalsky Sylvia G.,
Aladjem Mirit,
Barchan Dora,
Fuchs Sara
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80525-y
Subject(s) - acetylcholine receptor , nicotinic acetylcholine receptor , mongoose , binding site , chemistry , ligand (biochemistry) , nicotinic agonist , bungarotoxin , protein subunit , receptor , monoclonal antibody , binding domain , muscarinic acetylcholine receptor m5 , microbiology and biotechnology , biochemistry , antibody , biology , muscarinic acetylcholine receptor m3 , immunology , ecology , gene
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.