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Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A 2 homologue from Atropoides nummifer venom
Author(s) -
Murakami Mário T.,
Melo Cristiane C.,
Angulo Yamileth,
Lomonte Bruno,
Arni Raghuvir K.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106010700
Subject(s) - myotoxin , venom , snake venom , phospholipase a2 , phospholipase , biology , biochemistry , chemistry , enzyme
Lys49 snake‐venom phospholipase A 2 (PLA 2 ) 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 PLA 2 homologue from Atropoides nummifer , has been determined at 2.08 Å resolution and the anion‐binding site has been characterized.

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