دورية أكاديمية
Determination of the three-dimensional solution structure of scyllatoxin by 1H nuclear magnetic resonance.
| العنوان: | Determination of the three-dimensional solution structure of scyllatoxin by 1H nuclear magnetic resonance. |
|---|---|
| المؤلفون: | Martins JC; Vakgebied Biomoleculaire NMR, Vakgroep Organische Chemie, Universiteit Gent, Belgium., Van de Ven FJ, Borremans FA |
| المصدر: | Journal of molecular biology [J Mol Biol] 1995 Nov 03; Vol. 253 (4), pp. 590-603. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: Netherlands NLM ID: 2985088R Publication Model: Print Cited Medium: Print ISSN: 0022-2836 (Print) Linking ISSN: 00222836 NLM ISO Abbreviation: J Mol Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Amsterdam : Elsevier Original Publication: 1959- : London : Academic Press |
| مواضيع طبية MeSH: | Scorpion Venoms/*chemistry, Amino Acid Sequence ; Apamin/antagonists & inhibitors ; Apamin/chemistry ; Apamin/metabolism ; Binding, Competitive ; Calcium/metabolism ; Disulfides ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Potassium Channels/chemistry ; Potassium Channels/metabolism ; Protein Conformation ; Scorpion Venoms/metabolism ; Scorpion Venoms/pharmacology ; Sequence Homology, Amino Acid ; Solutions |
| مستخلص: | The three-dimensional solution structure of Scyllatoxin (leiurotoxin I) a venom peptide from the scorpion Leiurus quinquestriatus hebraeus was determined at 1 A resolution by homonuclear proton n.m.r. methods at 500 MHz. Data analysis and structure calculation followed conventional protocols inherent to DIANA and related programs with two exceptions. First, distance constraints were obtained from two-dimensional nuclear Overhauser spectra by a previously described partial relaxation matrix approach. Second, since the pairing pattern of the six cysteine residues was not established a priori, the unequivocal assignment of the disulfide bridges was achieved exclusively from the n.m.r. data by a statistical analysis of preliminary DIANA structures. In the final calculation we used 227 upper distance constraints, 67 torsional constraints from vicinal coupling constants and ten stereospecific assignments of beta-methylene protons. Scyllatoxin folds into a compact ellipsoidal shape. An alpha-helix (defined with 0.24 A resolution) spanning 2.5 turns from Leu5 till Ser14 is stabilized by Cys8-Cys26 and Cys12-Cys28 disulfide bridges to the carboxy-terminal strand of an anti-parallel beta-sheet. The antiparallel beta-sheet (defined at 0.66 A resolution) extends from Leu18 to Val29 with a tight turn at Gly23-Asp24 and displays a right-handed twist. Scyllatoxin competes with the toxins apamin from Apis mellifera mellifera and P05 from Androctonus mauretanicus mauretanicus for the same or similar high conductance calcium-activated potassium channels. Consideration of presently known biological activities and three-dimensional structures of these toxins suggest a different toxin-receptor interaction of scyllatoxin as compared to apamin and P05. |
| المشرفين على المادة: | 0 (Disulfides) 0 (Potassium Channels) 0 (Scorpion Venoms) 0 (Solutions) 0 (scorpion venom P05) 116235-63-3 (leiurotoxin I) 24345-16-2 (Apamin) SY7Q814VUP (Calcium) |
| تواريخ الأحداث: | Date Created: 19951103 Date Completed: 19951218 Latest Revision: 20131121 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1006/jmbi.1995.0575 |
| PMID: | 7473736 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 0022-2836 |
|---|---|
| DOI: | 10.1006/jmbi.1995.0575 |