TY - JOUR
T1 - α-Conotoxins
AU - Arias, Hugo R.
AU - Blanton, Michael P.
N1 - Funding Information:
This work was supported in part by NINDS Grant R29 NS35786 from the National Institutes of Health (to M.P. Blanton). We thank Dr Tina Machu for her critical reading of the manuscript.
PY - 2000/12/4
Y1 - 2000/12/4
N2 - α-Conotoxins (α-CgTxs) are a family of Cys-enriched peptides found in several marine snails from the genus Conus. These small peptides behave pharmacologically as competitive antagonists of the nicotinic acetylcholine receptor (AChR). The data indicate that (1) α-CgTxs are able to discriminate between muscle- and neuronal-type AChRs and even among distinct AChR subtypes; (2) the binding sites for α-CgTxs are located, like other cholinergic ligands, at the interface of α and non-α subunits (γ, δ, and ε for the muscle-type AChR, and β for several neuronal-type AChRs); (3) some α-CgTxs differentiate the high- from the low-affinity binding site found on either α/non-α subunit interface; and that (4) specific residues in the cholinergic binding site are energetically coupled with their corresponding pairs in the toxin stabilizing the α-CgTx-AChR complex. The α-CgTxs have proven to be excellent probes for studying the structure and function of the AChR family. (C) 2000 Elsevier Science Ltd.
AB - α-Conotoxins (α-CgTxs) are a family of Cys-enriched peptides found in several marine snails from the genus Conus. These small peptides behave pharmacologically as competitive antagonists of the nicotinic acetylcholine receptor (AChR). The data indicate that (1) α-CgTxs are able to discriminate between muscle- and neuronal-type AChRs and even among distinct AChR subtypes; (2) the binding sites for α-CgTxs are located, like other cholinergic ligands, at the interface of α and non-α subunits (γ, δ, and ε for the muscle-type AChR, and β for several neuronal-type AChRs); (3) some α-CgTxs differentiate the high- from the low-affinity binding site found on either α/non-α subunit interface; and that (4) specific residues in the cholinergic binding site are energetically coupled with their corresponding pairs in the toxin stabilizing the α-CgTx-AChR complex. The α-CgTxs have proven to be excellent probes for studying the structure and function of the AChR family. (C) 2000 Elsevier Science Ltd.
KW - α-Conotoxins
KW - Competitive antagonists
KW - Nicotinic acetylcholine receptors
UR - http://www.scopus.com/inward/record.url?scp=0033714035&partnerID=8YFLogxK
U2 - 10.1016/S1357-2725(00)00051-0
DO - 10.1016/S1357-2725(00)00051-0
M3 - Review article
C2 - 11091135
AN - SCOPUS:0033714035
VL - 32
SP - 1017
EP - 1028
JO - International Journal of Biochemistry and Cell Biology
JF - International Journal of Biochemistry and Cell Biology
SN - 1357-2725
IS - 10
ER -