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XB-ART-13217
Nat Neurosci 1998 Dec 01;18:668-74. doi: 10.1038/3669.
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Inhibition of T-type voltage-gated calcium channels by a new scorpion toxin.

Chuang RS , Jaffe H , Cribbs L , Perez-Reyes E , Swartz KJ .


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The biophysical properties of T-type voltage-gated calcium channels are well suited to pacemaking and to supporting calcium flux near the resting membrane potential in both excitable and non-excitable cells. We have identified a new scorpion toxin (kurtoxin) that binds to the alpha 1G T-type calcium channel with high affinity and inhibits the channel by modifying voltage-dependent gating. This toxin distinguishes between alpha 1G T-type calcium channels and other types of voltage-gated calcium channels, including alpha 1A, alpha 1B, alpha 1C and alpha 1E. Like the other alpha-scorpion toxins to which it is related, kurtoxin also interacts with voltage-gated sodium channels and slows their inactivation. Kurtoxin will facilitate characterization of the subunit composition of T-type calcium channels and help determine their involvement in electrical and biochemical signaling.

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