The ligand binding domain of the nicotinic acetylcholine receptor. Immunological analysis.
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.
Kachalsky
S G
SG
Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.
Aladjem
M
M
Barchan
D
D
Fuchs
S
S
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D001665:Binding Sites; D001666:Binding Sites, Antibody; D015153:Blotting, Western; D002038:Bungarotoxins / Q000378:metabolism; D003001:Cloning, Molecular; D008988:Herpestidae; D007163:Immunosorbent Techniques; D051379:Mice; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D011487:Protein Conformation; D011978:Receptors, Nicotinic / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014101:Torpedo
D000911:Antibodies, Monoclonal; D002038:Bungarotoxins; D010446:Peptide Fragments; D011978:Receptors, Nicotinic