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Titolo:
Diversification of neurotoxins by C-tail 'wiggling': a scorpion recipe forsurvival
Autore:
Gurevitz, M; Gordon, D; Ben-Natan, S; Turkov, M; Froy, O;
Indirizzi:
Tel Aviv Univ, George S Wise Fac Life Sci, Dept Plant Sci, IL-69978 Tel Aviv, Israel Tel Aviv Univ Tel Aviv Israel IL-69978 nt Sci, IL-69978 Tel Aviv, Israel Tel Aviv Univ, George S Wise Fac Life Sci, Dept Biochem, IL-69978 Tel Aviv, Israel Tel Aviv Univ Tel Aviv Israel IL-69978 iochem, IL-69978 Tel Aviv, Israel
Titolo Testata:
FASEB JOURNAL
fascicolo: 7, volume: 15, anno: 2001,
pagine: 1201 - 1205
SICI:
0892-6638(200105)15:7<1201:DONBC'>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANDROCTONUS-AUSTRALIS HECTOR; NUCLEAR-MAGNETIC-RESONANCE; TOXINS AFFECTING SODIUM; ALPHA-LIKE TOXIN; CHANNELS; POTASSIUM; SITE; DENDROTOXINS; EVOLUTION;
Keywords:
toxic polypeptides; scorpion neurotoxin; bioactive surface;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Gurevitz, M Tel Aviv Univ, George S Wise Fac Life Sci, Dept Plant Sci, Britania Bldg,Rm 506, IL-69978 Tel Aviv, Israel Tel Aviv Univ Britania Bldg,Rm506 Tel Aviv Israel IL-69978 l
Citazione:
M. Gurevitz et al., "Diversification of neurotoxins by C-tail 'wiggling': a scorpion recipe forsurvival", FASEB J, 15(7), 2001, pp. 1201-1205

Abstract

The structure of bioactive surfaces of proteins is a subject of intensive research, yet the mechanisms by which such surfaces have evolved are largely unknown. Polypeptide toxins produced by venomous animals such as sea anemones, cone snails, scorpions, and snakes show multiple routes for active site diversification, each maintaining a typical con served scaffold. Comparative analysis of an array of genetically related scorpion polypeptide toxins that modulate sodium channels in neuronal membranes suggests a unique route of toxic site diversification. This premise is based on recent identification of bioactive surfaces of toxin representative of three distinct pharmacological groups and a comparison of their 3-dimensional structures, Despite their similar scaffold, the bioactive surfaces of the various toxins vary considerably, but always coincide with the molecular exterior onto which the C-tail is anchored. Superposition of the toxin structures indicates that the C-tails diverge from a common structural start point, which suggests that the pharmacological versatility displayed by these toxins might have been achieved along evolution via structural reconfiguration of the C-tail, leading to reshaping of new bioactive surfaces.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 11:56:46