1q2k
From Proteopedia
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Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch
Overview
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.
About this Structure
1Q2K is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 00:19:58 2007
Categories: Single protein | Cai, Z. | Chi, C.W. | Lu, W. | Shi, Y. | Wu, J. | Xu, C. | Xu, Y. | Alpha-helix | Beta-sheet
