| Autor: |
Delatorre P; Departamento de Física--IBILCE, UNESP, São José Rio Preto, SP, Brazil., Olivieri JR, Ruggiero Neto J, Lorenzi CC, Canduri F, Fadel V, Konno K, Palma MS, Yamane T, de Azevedo WF Jr |
| Jazyk: |
angličtina |
| Zdroj: |
Biochimica et biophysica acta [Biochim Biophys Acta] 2001 Feb 09; Vol. 1545 (1-2), pp. 372-6. |
| DOI: |
10.1016/s0167-4838(00)00192-8 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
