Purification, crystallization and preliminary X-ray diffraction analysis of crotamine, a myotoxic polypeptide from the Brazilian snake Crotalus durissus terrificus.

Abstract

Crotamine, a highly basic myotoxic polypeptide (molecular mass 4881 Da) isolated from the venom of the Brazilian rattlesnake Crotalus durissus terrificus, causes skeletal muscle contraction and spasms, affects the functioning of voltage-sensitive sodium channels by inducing sodium influx and possesses antitumour activity, suggesting potential pharmaceutical applications. Crotamine was purified from C. durissus terrificus venom; the crystals diffracted to 1.9 Å resolution and belonged to the orthorhombic space group I2(1)2(1)2(1) or I222, with unit-cell parameters a = 67.75, b = 74.4, c = 81.01 Å. The self-rotation function indicated that the asymmetric unit contained three molecules. However, structure determination by molecular replacement using NMR-determined coordinates was unsuccessful and a search for potential derivatives has been initiated.

• Authors: Mônika A Coronado, Dessislava Georgieva, Friedrich Buck, Azat H Gabdoulkhakov, Anwar Ullah, Patrick J Spencer, Raghuvir K Arni, Christian Betzel
• Journal: Acta crystallographica. Section F, Structural biology and crystallization communications (Acta Crystallogr Sect F Struct Biol Cryst Commun) Vol. 68 Issue Pt 9 Pg. 1052-4 (Sep 01 2012) ISSN: 1744-3091 [Electronic] England
• PMID: 22949192 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Crotalid Venoms
• crotamine

Topics

• Animals
• Crotalid Venoms (chemistry, isolation & purification)
• Crotalus
• Crystallization
• Crystallography, X-Ray