Kaas Q et al. (2012) Nucleic Acids Res.

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Classification

• Gene superfamilies
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Introduction

Conotoxin name scheme

Targets of conotoxins

Post translational modifications of conotoxins and conopeptides

Recent key review articles

Conotoxin names

There are inconsistencies in the nomenclature used for naming conotoxins, but in general they tend to be named as follows. The initial categorization of the conopeptides is based on the pharmacological family they belong too and this is denoted by a Greek letter at the beginning of the peptide name. A letter or two is then used to designate the Conus species from which the peptide was isolated, followed by a Roman numeral specifying the disulfide bond connectivity. Conotoxins are also grouped into superfamilies, defined by their signal sequence in the initial prepropeptide and the disulfide framework.

Although peptides within the same superfamily have a particular disulfide bond framework, it is important to note that the number of residues between the cysteines may vary. The final letter in the name indicates the order of discovery within that category.

For example, vc1a can be decoded to yield the following information: it belongs to the alpha pharmacological family, has be been isolated from Conus victoriae, has a type 1 disulfide framework (superfamily A) and was the first peptide to be discovered in this category. Please see table one below for an example representations of the different superfamily disulfide bond scaffolds.

Please note: In the figure of conotoxin cystine frameworks the A- and T- superfamily share a similar framework but differ in the disulfide linkage pattern. The A-superfamily disulfide pattern is also referred to as globular fold whereas the T-superfamily pattern is the ribbon isoform. (When synthesizing peptides without distinct protective groups for the cysteines both isoforms may be obtained.) The M-, O- and P-superfamily share the same disulfide linkage patterns but differ in their cystine framework, i.e. the spacing between the cysteine residues.

For each superfamily, subtypes may occur which differ in the number of residues between the cysteines, for example the αA 4/7 subtype has four residues after the second cysteine (Cys^II) and seven residues after the third cysteine (Cys^III). In the T-superfamily spacing between Cys^III and Cys^IV may be two residues as in MrIA (type III framework) or no residues as in Lt5a (type V framework). A more detailed overview on the conotoxin frameworks can be found here.

Conotoxins can also have N- and C-terminal extensions like the 4/7 αA-conotoxin GID which has a N-terminal extension of four amino acids.