2aoz
From Proteopedia
Crystal structure of the myotoxin-II from Atropoides nummifer venom
Structural highlights
FunctionPA2HB_METNM Snake venom phospholipase A2 homolog that lacks enzymatic activity, but has myotoxic and cytolytic activities.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLys49 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. Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom.,Murakami MT, Melo CC, Angulo Y, Lomonte B, Arni RK Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 May 1;62(Pt, 5):423-6. Epub 2006 Apr 12. PMID:16682766[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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