Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
Data
2006-05-01
Autores
Murakami, Mário T. [UNESP]
Melo, Cristiane C. [UNESP]
Angulo, Yamileth
Lomonte, Bruno
Arni, Raghuvir K. [UNESP]
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Resumo
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 Å resolution and the anion-binding site has been characterized. © 2006 International Union of Crystallography. All rights reserved.
Descrição
Palavras-chave
Atropoides nummifer, myotoxin II, Atropoides nummifer, phospholipase A, snake venom, amino acid sequence, binding site, chemistry, crystallization, molecular genetics, sequence alignment, X ray crystallography, Amino Acid Sequence, Binding Sites, Crotalid Venoms, Crystallization, Crystallography, X-Ray, Molecular Sequence Data, Phospholipases A, Sequence Alignment
Como citar
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, v. 62, n. 5, p. 423-426, 2006.