ArticleBiophysical journal2000
Electrostatic interaction between charybdotoxin and a tetrameric mutant of Shaker K(+) channels.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Scorpion toxins prefer salt solutions.Journal of molecular modeling · 2015Article
- Stabilization of the conductive conformation of a voltage-gated K+ (Kv) channel: the lid mechanism.The Journal of biological chemistry · 2013Article
- A novel current pathway parallel to the central pore in a mutant voltage-gated potassium channel.The Journal of biological chemistry · 2011Article
- Structural basis for toxin resistance of beta4-associated calcium-activated potassium (BK) channels.The Journal of biological chemistry · 2008Article
- Probing the pH-dependent structural features of alpha-KTx12.1, a potassium channel blocker from the scorpion Tityus serrulatus.Protein science : a publication of the Protein Society · 2005Article
- Computational simulations of interactions of scorpion toxins with the voltage-gated potassium ion channel.Biophysical journal · 2004Article
- Tityustoxin-K(alpha) blockade of the voltage-gated potassium channel Kv1.3.British journal of pharmacology · 2003Article
- Inactivation and pharmacological properties of sqKv1A homotetramers in Xenopus oocytes cannot account for behavior of the squid "delayed rectifier" K(+) conductance.Biophysical journal · 2002Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The scorpion toxin, Charybdotoxin (CTX), blocks homotetrameric, voltage-gated K(+) channels by binding near the outer entrance to the pore in one of four indistinguishable orientations. We have determined the pH-dependence of CTX block of a tetrameric Shaker potassium channel with a single copy of a histidine replacing the wild-type phenylalanine at position 425. We compared this pH-dependence with that from homotetrameric channels with four copies of the mutation. We found that protonation of a single amino acid at position 425 had a large effect on the affinity of the channel for CTX-much larger than expected if only one of the four CTX binding orientations was disrupted. The pK(a) for the H(+)-ion induced protection from CTX block indicates that the electrostatic environment near position 425 is likely basic in nature, perhaps because of the proximity of lysine 427. We also examined the pH-dependence of block of channels with one and four copies of the histidine mutation by CTX containing neutralizing mutations of four basic residues on the active face of the toxin. The results suggested an orientation of CTX on the channel that places three of the positively charged CTX residues very near three of the four Shaker 425 positions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.