1q2k

Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi KarschSolution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch

Structural highlights 1q2k is a 1 chain structure with sequence from Mesobuthus martensii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 21 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KA191_MESMA Selective inhibitor of high conductance calcium-activated potassium channels KCa1.1/KCNMA1. May be insect specific. [PDB:3E8Y] Publication Abstract from PubMed BmBKTx1 is a 31-amino acid peptide identified from the venom of the Chinese scorpion Buthus martensi Karsch, blocking high-conductance calcium-activated potassium channels. Sequence homology analysis indicates that BmBKTx1 is a new subfamily of short-chain alpha-KTx toxins of the potassium channel, which we term alpha-KTx19. Synthetic BmBKTx1 was prepared by using solid-phase peptide synthesis. Two-dimensional NMR spectroscopy techniques were used to determine the solution structure of BmBKTx1. The results show that the BmBKTx1 forms a typical cysteine-stabilized alpha/beta scaffold adopted by most short-chain scorpion toxins. The structure of BmBKTx1 consists of a two-stranded antiparallel beta-sheet (residues 20-29) and an alpha-helix (residues 5-15). The three-dimensional structure of BmBKTx1 was also compared with those of two function-related scorpion toxins, charybdotoxin (ChTx) and BmTx1, and their structural and functional implications are discussed. Solution structure of BmBKTx1, a new BKCa1 channel blocker from the Chinese scorpion Buthus martensi Karsch.,Cai Z, Xu C, Xu Y, Lu W, Chi CW, Shi Y, Wu J Biochemistry. 2004 Apr 6;43(13):3764-71. PMID:15049683 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Potassium channel toxin 3D structures

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