1wm7
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Solution Structure of BmP01 from the Venom of Scorpion Buthus martensii Karsch, 9 structures
OverviewOverview
From 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.
About this StructureAbout this Structure
1WM7 is a Single protein structure of sequence from Mesobuthus martensii. Full crystallographic information is available from OCA.
ReferenceReference
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
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