mu-conotoxin Chemische Eigenschaften,Einsatz,Produktion Methoden
Beschreibung
Mu-conotoxins are a family of peptides from the venoms of predatory cone snails. Conotoxins, which are peptides consisting of 10 to 30 amino acid residues, typically have one or more disulfide bonds. Conotoxins have a variety of mechanisms of actions, most of which have not been determined. Mu-conotoxins have two types of cysteine arrangements, but the knottin scaffold is not observed.
Structure and conformation
mu-Conotoxin (µ-CTX) is a receptor site I sodium channel blocker isolated from the sea snail Conus geographus that specifically inhibits Na+ flux in skeletal muscle and eel Na+ channels with high affinity by physically occluding the channel pore. µ-CTXs are peptides consisting of 22 amino acid residues with six cysteines that form three internal disulfide bonds, imparting extreme rigidity to the toxin molecule. The toxin contains a number of charged residues, including several positively-charged amino acids that have been shown to be critical for its biological activity. At physiological pH, the toxin carries a net charge of +6 or +7 respectively for the GIIIA and GIIIB subtypes. The three-dimensional structure of µ CTX resembles a tetragonal bipyramid with axial distances of approximately 25 and 20 Å.
mu-conotoxin Upstream-Materialien And Downstream Produkte
Upstream-Materialien
Downstream Produkte
