Publication Date:
1987-01-02
Description:
The alpha-chain of the nicotinic acetylcholine receptor carries the binding sites both for cholinergic ligands and for most experimentally induced or naturally occurring antibodies to the native receptor. By means of expression cloning in Escherichia coli, fusion proteins were derived from specific fragments of a complementary DNA encoding the mouse alpha-chain, allowing the mapping of the toxin-binding site to residues 160-216 and the main immunogenic region to residues 6-85. This approach permits the independent study of different functional domains of a complex receptor molecule and should be generally applicable to other proteins for which complementary DNA clones are available.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barkas, T -- Mauron, A -- Roth, B -- Alliod, C -- Tzartos, S J -- Ballivet, M -- New York, N.Y. -- Science. 1987 Jan 2;235(4784):77-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2432658" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Antibodies, Monoclonal/immunology
;
Binding Sites
;
Binding, Competitive
;
Bungarotoxins/metabolism
;
Cloning, Molecular
;
Epitopes
;
Humans
;
Immunosorbent Techniques
;
Ligands
;
Mice
;
Receptors, Nicotinic/genetics/*immunology
;
Recombinant Fusion Proteins/immunology
;
Species Specificity
;
Structure-Activity Relationship
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
