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...

Full description

Saved in:
Bibliographic Details
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
Subjects
Acetylcholine receptor
Ligand binding site
Monoclonal antibody 5.5
α-Bungarotoxin
Online AccessGet full text

Cover

More Information
Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(93)80525-Y