α-Conotoxins

Hugo R. Arias, Michael P. Blanton

Research output: Contribution to journalReview article

59 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1017-1028
Number of pages12
JournalInternational Journal of Biochemistry and Cell Biology
Volume32
Issue number10
DOIs
StatePublished - 4 Dec 2000
Externally publishedYes

Fingerprint

Conotoxins
Cholinergic Receptors
Binding Sites
Cholinergic Agents
Muscle
Conus Snail
Muscles
Peptides
Nicotinic Receptors
Ligands

Keywords

  • α-Conotoxins
  • Competitive antagonists
  • Nicotinic acetylcholine receptors

Cite this

Arias, Hugo R. ; Blanton, Michael P. / α-Conotoxins. In: International Journal of Biochemistry and Cell Biology. 2000 ; Vol. 32, No. 10. pp. 1017-1028.
@article{7f311a7f8e9945aaadd7f67b073e1579,
title = "α-Conotoxins",
abstract = "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.",
keywords = "α-Conotoxins, Competitive antagonists, Nicotinic acetylcholine receptors",
author = "Arias, {Hugo R.} and Blanton, {Michael P.}",
year = "2000",
month = "12",
day = "4",
doi = "10.1016/S1357-2725(00)00051-0",
language = "English",
volume = "32",
pages = "1017--1028",
journal = "International Journal of Biochemistry and Cell Biology",
issn = "1357-2725",
number = "10",

}

α-Conotoxins. / Arias, Hugo R.; Blanton, Michael P.

In: International Journal of Biochemistry and Cell Biology, Vol. 32, No. 10, 04.12.2000, p. 1017-1028.

Research output: Contribution to journalReview article

TY - JOUR

T1 - α-Conotoxins

AU - Arias, Hugo R.

AU - Blanton, Michael P.

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 -