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Purification, crystallization and preliminary X-ray diffraction analysis of crotamine, a myotoxic polypeptide from the Brazilian snake Crotalus durissus terrificus
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 possess...
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Published in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2012-09, Vol.68 (9), p.1052-1054 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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 I212121 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. |
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ISSN: | 1744-3091 1744-3091 2053-230X |
DOI: | 10.1107/S1744309112032721 |