1t1t
From Proteopedia
Jump to navigationJump to search
Solution Structure of Kurtoxin
| ||||||||||||
Structural highlights
FunctionKURT_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
| ||||||||||||||||||
This page was last modified 04:54, 17 October 2024.