Preliminary cryocrystallography analysis of an eumenine mastoparan toxin isolated from the venom of the wasp Anterhynchium flavomarginatum micado.
Biochim Biophys Acta
; 1545(1-2): 372-6, 2001 Feb 09.
Article
em En
| MEDLINE
| ID: mdl-11342062
ABSTRACT
Mastoparans are tetradecapeptides found to be the major component of vespid venoms. These peptides present a wide spectrum of biological activities, such as mast cell degranulation, hemolytic activity and also reveals antimicrobial activity. A mastoparan toxin isolated from the venom of Anterhynchium flavomarginatum micado has been crystallized. At room temperature these crystals diffracted to 2.8 A resolution. However, upon cooling to cryogenic temperature around 85 K, the original resolution limit could be improved to 2.0 A. Crystals were determined to belong to the space group P3(1) (P3(2)). This is the first mastoparan to be crystallized and it will provide further insights in the conformational significance of mastoparan toxins, with respect to their potency and activity in G protein regulation.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Venenos de Vespas
/
Vespas
/
Cristalografia por Raios X
/
Proteínas de Insetos
Limite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
2001
Tipo de documento:
Article
País de afiliação:
Brasil