Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 1 de 1
Filter
Add more filters











Database
Language
Publication year range
1.
Peptides ; 46: 40-6, 2013 Aug.
Article in English | MEDLINE | ID: mdl-23684923

ABSTRACT

Opisthacanthus cayaporum belongs to the Liochelidae family, and the scorpions from this genus occur in southern Africa, Central America and South America and, therefore, can be considered a true Gondwana heritage. In this communication, the isolation, primary structure characterization, and K⁺-channel blocking activity of new peptide from this scorpion venom are reported. OcyKTx2 is a 34 amino acid long peptide with four disulfide bridges and molecular mass of 3807 Da. Electrophysiological assays conducted with pure OcyKTx2 showed that this toxin reversibly blocks Shaker B K⁺-channels with a Kd of 82 nM, and presents an even better affinity toward hKv1.3, blocking it with a Kd of ∼18 nM. OcyKTx2 shares high sequence identity with peptides belonging to subfamily 6 of α-KTxs that clustered very closely in the phylogenetic tree included here. Sequence comparison, chain length and number of disulfide bridges analysis classify OcyKTx2 into subfamily 6 of the α-KTx scorpion toxins (systematic name, α-KTx6.17).


Subject(s)
Kv1.3 Potassium Channel/antagonists & inhibitors , Peptides/metabolism , Scorpion Venoms/metabolism , Shaker Superfamily of Potassium Channels/antagonists & inhibitors , Amino Acid Sequence , Animals , Cells, Cultured , Humans , Intercellular Signaling Peptides and Proteins , Peptides/chemistry , Peptides/isolation & purification , Potassium Channel Blockers/chemistry , Potassium Channel Blockers/isolation & purification , Potassium Channel Blockers/metabolism , Protein Binding , Scorpion Venoms/chemistry , Scorpion Venoms/isolation & purification , Scorpions/metabolism , Sequence Alignment , Sequence Analysis, Protein
SELECTION OF CITATIONS
SEARCH DETAIL