1wm7
Solution Structure of BmP01 from the Venom of Scorpion Buthus martensii Karsch, 9 structuresSolution Structure of BmP01 from the Venom of Scorpion Buthus martensii Karsch, 9 structures
Structural highlights
FunctionKAX82_MESMA Blocks small conductance calcium-activated potassium channels (KCNN, SK). Low toxicity by intracerebroventricular injection into mice.[1] Publication Abstract from PubMedFrom the venom of scorpion Buthus martensii Karsch,a short peptide (BmP01, 29 amino acid residues) was isolated and characterized as previously reported (Lebren, R. R., et al. (1997) Eur. J. Biochem. 245, 457-464). It was shown to reduce 33% outward K(+) channel (hippocampal neurons) currents at 10 microM. The solution structure of BmP01 was determined by 2D (1)H NMR spectroscopy. The NOEs, coupling constants, and H-D exchange obtained from NMR spectroscopy were used in structural calculations. The conformation of BmP01 is composed of a short alpha-helix (Cys 3-Thr 12) and a two-stranded antiparallel beta-sheet (Ala 15-Asp 20 and Lys 23-Pro 28). There are three disulfide bridges (Cys 3-Cys 19, Cys 6-Cys 24 and Cys 10-Cys 26) connecting the alpha-helix and beta-sheet. Asp 20 to Lys 23 form a type II turn linking the two strands. Structural and electrostatic potential comparison between BmP01 and its analogues are also presented. Solution structure of BmP01 from the venom of scorpion Buthus martensii Karsch.,Wu G, Li Y, Wei D, He F, Jiang S, Hu G, Wu H Biochem Biophys Res Commun. 2000 Oct 5;276(3):1148-54. PMID:11027603[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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