Structural highlights
Function
KURT_PARTR Alpha toxins bind voltage-independently at site-3 of sodium channels and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin acts on Nav1.2/SCN2A. Also binds to Cav3.1/CACNA1G and Cav3.2/CACNA1H T-type calcium channels with high affinity and inhibits the channels by modifying voltage-dependent gating. Another study (PubMed:11896142) shows that it also targets neuronal high-threshold calcium channels, including P-type, N-type, and L-type calcium channels (Cav), and others that still are unidentified pharmacologically.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Chuang RS, Jaffe H, Cribbs L, Perez-Reyes E, Swartz KJ. Inhibition of T-type voltage-gated calcium channels by a new scorpion toxin. Nat Neurosci. 1998 Dec;1(8):668-74. PMID:10196582 doi:http://dx.doi.org/10.1038/3669
- ↑ Sidach SS, Mintz IM. Kurtoxin, a gating modifier of neuronal high- and low-threshold ca channels. J Neurosci. 2002 Mar 15;22(6):2023-34. PMID:11896142
