Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom


Autoria(s): Murakami, Mário T.; Melo, Cristiane C.; Angulo, Yamileth; Lomonte, Bruno; Arni, Raghuvir K.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

27/05/2014

27/05/2014

01/05/2006

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