Abstract

Abstract Crotalase is a serine protease from eastern diamondback rattlesnake ( Crotalus adamanteus ) venom. Crotalase has high amino-acid sequence similarity to three other members of the serine protease family, α-thrombin, β-trypsin and kallikrein A. Their structural information was used to predict the folding of crotalase. The computational structural data were used to explain biochemical properties of this important enzyme. The first computational model for the structure of crotalase is reported herein. The implications of the details of the structure for the biological activity are discussed.

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