Synthesis, 1H NMR structure, and activity of a three-disulfide-bridged maurotoxin analog designed to restore the consensus motif of scorpion toxins
Z Fajloun, G Ferrat, E Carlier, M Fathallah… - Journal of Biological …, 2000 - ASBMB
Maurotoxin (MTX) is a 34-residue toxin that has been isolated from the venom of the
chactidae scorpionScorpio maurus palmatus. The toxin displays an exceptionally wide
range of pharmacological activity since it binds onto small conductance Ca 2+-activated K+
channels and also blocks Kv channels (Shaker, Kv1. 2 and Kv1. 3). MTX possesses 53–68%
sequence identity with HsTx1 and Pi1, two other K+ channel short chain scorpion toxins
cross-linked by four disulfide bridges. These three toxins differ from other K+/Cl−/Na+ …
chactidae scorpionScorpio maurus palmatus. The toxin displays an exceptionally wide
range of pharmacological activity since it binds onto small conductance Ca 2+-activated K+
channels and also blocks Kv channels (Shaker, Kv1. 2 and Kv1. 3). MTX possesses 53–68%
sequence identity with HsTx1 and Pi1, two other K+ channel short chain scorpion toxins
cross-linked by four disulfide bridges. These three toxins differ from other K+/Cl−/Na+ …
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