1Q2K

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

Summary for 1Q2K

• Entry DOI: 10.2210/pdb1q2k/pdb
• Descriptor: Neurotoxin BmK37 (1 entity in total)
• Functional Keywords: alpha-helix, beta-sheet, toxin
• Cellular location: Secreted: P83407
• Total number of polymer chains: 1
• Total formula weight: 3348.02

Authors

Cai, Z.,Xu, C.,Xu, Y.,Lu, W.,Chi, C.W.,Shi, Y.,Wu, J. (deposition date: 2003-07-25, release date: 2003-09-09, Last modification date: 2024-10-09)

Primary citation

Cai, Z.,Xu, C.,Xu, Y.,Lu, W.,Chi, C.W.,Shi, Y.,Wu, J.
Solution Structure of BmBKTx1, a New BK(Ca)(1) Channel Blocker from the Chinese Scorpion Buthus martensi Karsch(,).
Biochemistry, 43:3764-3771, 2004

PubMed Abstract: 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.

PubMed: 15049683
DOI: 10.1021/bi035412+

Experimental method

SOLUTION NMR