Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
27/05/2014
27/05/2014
01/05/2006
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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. |
Formato |
423-426 |
Identificador |
http://dx.doi.org/10.1107/S1744309106010700 http://www.ncbi.nlm.nih.gov/pubmed/16682766 Acta Crystallographica Section F: Structural Biology and Crystallization Communications, v. 62, n. 5, p. 423-426, 2006. 1744-3091 http://hdl.handle.net/11449/68864 10.1107/S1744309106010700 http://www.ncbi.nlm.nih.gov/pubmed/16682766 WOS:000237159000001 2-s2.0-33646836252 WOS000237159000001.pdf |
Idioma(s) |
eng |
Relação |
Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Direitos |
openAccess |
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 |
Tipo |
info:eu-repo/semantics/article |