ArticleJournal of biomedicine & biotechnology2011
Both basic and acidic amino acid residues of IpTx(a) are involved in triggering substate of RyR1.
Article in Journal of biomedicine & biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Cryo-EM analysis of scorpion toxin binding to Ryanodine Receptors reveals subconductance that is abolished by PKA phosphorylation.Science advances · 2023Article
- Scorpion Peptides and Ion Channels: An Insightful Review of Mechanisms and Drug Development.Toxins · 2023Review
- Structure-function relationships of peptides forming the calcin family of ryanodine receptor ligands.The Journal of general physiology · 2016Article
- Scorpion venom components that affect ion-channels function.Toxicon : official journal of the International Society on Toxinology · 2013Review
- Multiple actions of phi-LITX-Lw1a on ryanodine receptors reveal a functional link between scorpion DDH and ICK toxins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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Authors and funding
4 authors.
Funding
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Abstract
Imperatoxin A (IpTx(a)) is known to modify the gating of skeletal ryanodine receptor (RyR1). In this paper, the ability of charged aa residues of IpTx(a) to induce substate of native RyR1 in HSR was examined. Our results show that the basic residues (e.g., Lys¹⁹, Lys²⁰, Lys²², Arg²³, and Arg²⁴) are important for producing substate of RyR1. In addition, other basic residues (e.g., Lys³⁰, Arg³¹, and Arg³³ near the C-terminus and some acidic residues (e.g., Glu²⁹, Asp¹³, and Asp²) are also involved in the generation of substate. Residues such as Lys⁸ and Thr²⁶ may be involved in the self-regulation of substate of RyR1, since alanine substitution of the aa residues led to a drastic conversion to the substate. The modifications of the channel gating by the wild-type and mutant toxins were similar in purified RyR1. Taken together, the specific charge distributions on the surface of IpTx(a) are essential for regulation of the channel gating of RyR1.
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