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2006•Acta Crystallographica Section F Structural Biology and Crystallization CommunicationsOpen access

Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2homologue fromAtropoides nummifervenom

M.T. Murakami, Cristiane C. de Melo, Yamileth Angulo, Bruno Lomonte, Raghuvir K. Arni

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Abstract

Lys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic proteins which, although lacking catalytic activity, possess the ability to disrupt biological membranes, inducing significant muscle-tissue loss and permanent disability in severely envenomed patients. Since the structural basis for their toxic activity is still only partially understood, the structure of myotoxin II, a monomeric Lys49 PLA2 homologue from Atropoides nummifer, has been determined at 2.08 angstroms resolution and the anion-binding site has been characterized.

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Lys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic proteins which, although lacking catalytic activity, possess the ability to disrupt biological membranes, inducing significant muscle-tissue loss and permanent disability in severely envenomed patients. Since the structural basis for their toxic activity is still only partially understood, the structure of myotoxin II, a monomeric Lys49 PLA2 homologue from Atropoides nummifer, has been determined at 2.08 angstroms resolution and the anion-binding site has been characterized.

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Available abstract

Lys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic proteins which, although lacking catalytic activity, possess the ability to disrupt biological membranes, inducing significant muscle-tissue loss and permanent disability in severely envenomed patients. Since the structural basis for their toxic activity is still only partially understood, the structure of myotoxin II, a monomeric Lys49 PLA2 homologue from Atropoides nummifer, has been determined at 2.08 angstroms resolution and the anion-binding site has been characterized.

Key concepts: Myotoxin, Venom, Snake venom, Phospholipase A2, Phospholipase, Biology, Biochemistry, Chemistry

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