Structural highlights
Function
VKT9_BUNFA Dual-function toxin that inhibits both serine proteases (high activity on chymotrypsin (Ki = 18 nM), and low activity on elastase) and voltage-gated potassium channels Kv1.3/KCNA3 (IC(50) = 120.0 nM).[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
- ↑ Chen C, Hsu CH, Su NY, Lin YC, Chiou SH, Wu SH. Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the elapid snake Bungarus fasciatus. J Biol Chem. 2001 Nov 30;276(48):45079-87. Epub 2001 Sep 18. PMID:11562364 doi:10.1074/jbc.M106182200
- ↑ Yang W, Feng J, Wang B, Cao Z, Li W, Wu Y, Chen Z. BF9, the first functionally characterized snake toxin peptide with Kunitz-type protease and potassium channel inhibiting properties. J Biochem Mol Toxicol. 2014 Feb;28(2):76-83. doi: 10.1002/jbt.21538. Epub 2013, Nov 14. PMID:24243656 doi:http://dx.doi.org/10.1002/jbt.21538
