Structural highlights
Function
VKT1A_CYRSC Dual-function toxin that inhibits both serine proteases (trypsin) and voltage-gated potassium channels (Kv). The toxin is more active on Kv1.1/KCNA1 (78% inhibition), than on Kv1.2/KCNA2 (10% inhibition), and Kv1.3/KCNA3 (28% inhibition), although a high dose (5 uM) is needed. The inhibition of potassium channels is voltage-dependent.[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
- ↑ Liang S. An overview of peptide toxins from the venom of the Chinese bird spider Selenocosmia huwena Wang [=Ornithoctonus huwena (Wang)]. Toxicon. 2004 Apr;43(5):575-85. PMID:15066414 doi:http://dx.doi.org/10.1016/j.toxicon.2004.02.005
- ↑ Peng K, Lin Y, Liang SP. Nuclear magnetic resonance studies on huwentoxin-XI from the Chinese bird spider Ornithoctonus huwena: 15N labeling and sequence-specific 1H, 15N nuclear magnetic resonance assignments. Acta Biochim Biophys Sin (Shanghai). 2006 Jul;38(7):457-66. PMID:16820861
