Functional consequences of deleting the two C-terminal residues of the scorpion toxin BmTX3

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1646, Issue 1-2, 2003, Pages 152-156

  Vacher, Hélène ^a   Romi Lebrun, Régine ^b   Crest, Marcel ^c   Masmejean, Frédérique ^d   Bougis, Pierre E ^a   Darbon, Hervé ^e   Martin Eauclaire, Marie France ^a  

^a CNRS   (France)

^b CNRS and Aix Marseille University   (France)

^c AIX MARSEILLE UNIVERSITY   (France)

^d LNCF CNRS   (France)

^e Centre National de la Recherche Scientifique   (France)

Author keywords

A type K+ current; Binding; Deletion; Scorpion toxin

Indexed keywords

BMTX3 TOXIN; TOXIN; UNCLASSIFIED DRUG; POTASSIUM CHANNEL; SCORPION VENOM; TX3 TOXIN, BUTHUS MARTENSII; TYROSINE;

ANIMAL CELL; ARTICLE; BINDING ASSAY; BRAIN MEMBRANE; CARBOXY TERMINAL SEQUENCE; CONCENTRATION RESPONSE; CONTROLLED STUDY; CORPUS STRIATUM; EXPERIMENTAL TEST; GENE DELETION; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR MECHANICS; NERVE CELL CULTURE; NONHUMAN; PATCH CLAMP; POTASSIUM CURRENT; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTON NUCLEAR MAGNETIC RESONANCE; RECEPTOR BLOCKING; SCORPION; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; ANIMAL; BINDING COMPETITION; BRAIN; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RAT; SYNAPTOSOME;

SCORPIONES;

AMINO ACID SEQUENCE; ANIMALS; BINDING, COMPETITIVE; BRAIN; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POTASSIUM CHANNELS; RATS; SCORPION VENOMS; SYNAPTOSOMES; TYROSINE;

EID: 0043123414     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(02)00557-5     Document Type: Article

References (19)

1. Goudet C., Chi C.W., Tytgat J. An overview of toxins and genes from the venom of the Asian scorpion Buthus martensi Karsch. Toxicon. 40:2002;1239-1258.
2. Vacher H., Romi-Lebrun R., Mourre C., Lebrun B., Kourrich S., Masmejean F., Nakajima T., Legros C., Crest M., Bougis P.E., Martin-Eauclaire M.F. A new class of scorpion toxin binding sites related to an A-type K+ channel: pharmacological characterization and localization in rat brain. FEBS Lett. 501:2001;31-36.
3. Pisciotta M., Coronas F.I., Bloch C., Prestipino G., Possani L.D. Fast K(+) currents from cerebellum granular cells are completely blocked by a peptide purified from Androctonus australis Garzoni scorpion venom. Biochim. Biophys. Acta. 1468:2000;203-212.
4. Vacher H., Alami M., Crest M., Possani L.D., Bougis P.E., Martin-Eauclaire M.F. Expanding the scorpion toxin α-KTX 15 family with AmmTX3 from Androctonus mauretanicus. Eur. J.Biochim. 269:2002;6037-6041.
5. Darbon H., Blanc E., Sabatier J.M. Three-dimentional structure of scorpion toxins: Towards a new model of interaction with potassium channels. Martin Y.C. Perspectives in Drug Discover and Design. vols. 15/16:1999;41-46 Kluwer Academic Publisher.
6. Aiyar J., Withka J.M., Rizzi J.P., Singleton D.H., Andrews G.C., Lin W., Boyd J., Hanson D.C., Simon M., Dethlefs B.et al. Topology of the pore-region of a K+ channel revealed by the NMR-derived structures of scorpion toxins. Neuron. 15:1995;1169-1181.
7. Gross A., MacKinnon R. Agitoxin footprinting the shaker potassium channel pore. Neuron. 16:1996;399-406.
8. Goldstein S.A., Pheasant D.J., Miller C. The charybdotoxin receptor of a Shaker K+ channel: peptide and channel residues mediating molecular recognition. Neuron. 12:1994;1377-1388.
9. Dauplais M., Lecoq A., Song J., Cotton J., Jamin N., Gilquin B., Roumestand C., Vita C., de Medeiros C.L.C., Rowan E.G., Harvey A.L., Menez A. On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures. J. Biol. Chem. 272:1997;4302-4309.
10. Alessandri-Haber N., Lecoq A., Gasparini S., Grangier-Macmath G., Jacquet G., Harvey A.L., de Medeiros C., Rowan E.G., Gola M., Menez A., Crest M. Mapping the functional anatomy of BgK on Kv1.1, Kv1.2, and Kv1.3. Clues to design analogs with enhanced selectivity. J. Biol. Chem. 274:1999;35653-35661.
11. Bednarek M.A., Bugianesi R.M., Leonard R.J., Felix J.P. Chemical synthesis and structure-function studies of margatoxin, a potent inhibitor of voltage-dependent potassium channel in human T lymphocytes. Biochem. Biophys. Res. Commun. 198:1994;619-625.
12. Romi-Lebrun R., Lebrun B., Martin-Eauclaire M.F., Ishiguro M., Escoubas P., Wu F.Q., Hisada M., Pongs O., Nakajima T. Purification, characterization, and synthesis of three novel toxins from the Chinese scorpion Buthus martensi, which act on K+ channels. Biochemistry. 36:1997;13473-13482.
13. Pimenta A.M., Stocklin R., Favreau P., Bougis P.E., Martin-Eauclaire M.F. Moving pieces in a proteomic puzzle: mass fingerprinting of toxic fractions from the venom of Tityus serrulatus (Scorpiones, Buthidae). Rapid Commun. Mass Spectrom. 15:2001;1562-1572.
14. Blanc E., Romi-Lebrun R., Bornet O., Nakajima T., Darbon H. Solution structure of two new toxins from the venom of the Chinese scorpion Buthus martensi Karsch blockers of potassium channels. Biochemistry. 37:1998;12412-12418.
15. Kowalski C., Crest M., Vuillet J., Pin T., Gola M., Nieoullon A. Emergence of a synaptic neuronal network within primary striatal cultures seeded in serum-free medium. Neuroscience. 64:1995;979-993.
16. Tytgat J., Chandy K.G., Garcia M.L., Gutman G.A., Martin-Eauclaire M.F., van der Walt J.J., Possani L.D. A unified nomenclature for short-chain peptides isolated from scorpion venoms: alpha-KTx molecular subfamilies. Trends Pharmacol. Sci. 20:1999;444-447.
17. Lipkind G.M., Fozzard H.A. A model of scorpion toxin binding to voltage-gated K+ channels. J. Membr. Biol. 158:1997;187-196.
18. Quiram P.A., Sine S.M. Structural elements in alpha-conotoxin ImI essential for binding to neuronal alpha receptors. J. Biol. Chem. 273:1998;11007-11011.
19. Flinn J.P., Pallaghy P.K., Lew M.J., Murphy R., Angus J.A., Norton R.S. Roles of key functional groups in omega-conotoxin GVIA synthesis, structure and functional assay of selected peptide analogues. Eur. J. Biochem. 262:1999;447-455.