LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Conserved_site |
| Description | Cone snail toxins, conotoxins, are small peptides with disulphide connectivity, that target ion-channels or G-protein coupled receptors. Based on the numberand pattern of disulphide bonds and biological activities, conotoxins can be classified into several families []. Omega and delta families of conotoxinshave a knottin or inhibitor cystine knot scaffold. The knottin scaffold is a very special disulphide through disulphide knot, in which the III-VI disulphidebond crosses the macrocycle formed by two other disulphide bonds (I-IV and II- V) and the interconnecting backbone segments, where I-VI indicates the sixcysteine residues starting from the N terminus. Conotoxins represent a unique arsenal of neuropharmacologically active peptides that have been evolutionarily tailored to afford unprecedented andexquisite selectivity for a wide variety of ion-channel subtypes. The toxins derived from cone snails are currently being investigated for the treatment ofchronic pain, epilepsy, cardiovascular diseases, psychiatric and movement disorders, spasticity, cancer, stroke as well as an anesthetic agent. Severalpotential analgesic and anti-inflammatory peptides from conotoxin family have been identified and patented [], []:Conus magus (Magus cone) (Magician's cone snail) omega-conotoxin MVIIa (Ziconotide) is used for the treatment of chronic pain.Conus catus (Cat cone) omega-conotoxin CVID is tested for treating severe morphine- resistant pain stress.Conus geographus (Geography cone) (Nubecula geographus) omega-conotoxin GVIA may exert antagonistic effects against beta-endorphin induced anti-nociception.The cysteine arrangement [C-C-CC-C-C] is the same for omega and deltafamilies, but omega conotoxins are calcium channel blockers whereas delta conotoxins delay the inactivation of sodium channels. The disulphidebonding network as well as specific amino acids in inter-cysteine loops provide specificity of conotoxin []. Two signature patterns were developedfor omega and delta conotoxin families. The patterns each include six conserved cysteines thought to be important for the maintenance of thetertiary structure of the conotoxins. This entry represents the delta-conotoxins. |
| Short Name | Conotoxin_d-typ_CS |
