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Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom.

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.

SUBMITTER: Murakami MT

PROVIDER: S-EPMC2219968 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature

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Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom.

Murakami Mário T MT Melo Cristiane C CC Angulo Yamileth Y Lomonte Bruno B Arni Raghuvir K RK

Acta crystallographica. Section F, Structural biology and crystallization communications 20060412 Pt 5

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 resolutio ...[more]

PMID: 16682766

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