Structural highlights
Function
[PA2HB_ATRNM] 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 PubMed
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.
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 Also
References
- ↑ Angulo Y, Olamendi-Portugal T, Alape-Giron A, Possani LD, Lomonte B. Structural characterization and phylogenetic relationships of myotoxin II from Atropoides (Bothrops) nummifer snake venom, a Lys49 phospholipase A(2) homologue. Int J Biochem Cell Biol. 2002 Oct;34(10):1268-78. PMID:12127577
- ↑ Murakami MT, Melo CC, Angulo Y, Lomonte B, Arni RK. Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 May 1;62(Pt, 5):423-6. Epub 2006 Apr 12. PMID:16682766 doi:http://dx.doi.org/10.1107/S1744309106010700
