2jot
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Nuclear Magnetic Resonance Studies on Huwentoxin-XI from the Chinese Bird Spider Ornithoctonus huwena
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Structural highlights
FunctionVKT1A_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
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This page was last modified 09:13, 6 November 2024.